Histidyl conformations and short N–H<sup>...</sup>N hydrogen bonds: Structure of <scp>D</scp>,<scp>L</scp>-histidyl-<scp>L</scp>,<scp>D</scp>-histidine pentahydrate

Krause, Jeanette A.; Baures, Paul W.; Eggleston, Drake S.

doi:10.1107/s0108768191000915

Cited by 18 publications

(12 citation statements)

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“…Such interactions have been studied by using imidazole and imidazolium, which form cocrystals displaying a strong hydrogen bond (42), and modeling them computationally (43). In addition, this imidazoleimidazolium sample and other complexes (44) have been extensively studied by solid-state NMR (45,46). The presence of a low-barrier hydrogen bond is characterized by an increase in the frequency of the protonated 15 N resonance, a decrease in the nonprotonated resonant frequency, and broadening of the resonances.…”

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confidence: 99%

Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity

Nishimura

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

245

450

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The heart of the H ؉ conductance mechanism in the homotetrameric M2 H ؉ channel from influenza A is a set of four histidine side chains. Here, we show that protonation of the third of these imidazoles coincides with acid activation of this transmembrane channel and that, at physiological pH, the channel is closed by two imidazole-imidazolium dimers, each sharing a low-barrier hydrogen bond. This unique construct succeeds in distributing a pair of charges over four rings and many atoms in a low dielectric environment to minimize charge repulsion. These dimers form with identical pK as of 8.2 ؎ 0.2, suggesting cooperative H ؉ binding and clearly illustrating high H ؉ affinity for this channel. The protonation behavior of the histidine side chains has been characterized by using solid-state NMR spectroscopy on the M2 transmembrane domain in fully hydrated lipid bilayers where the tetrameric backbone structure is known. Furthermore, electrophysiological measurements of multichannel and single-channel experiments confirm that these protein constructs are functional.M2 channel ͉ proton channel ͉ solid-state NMR ͉ low-barrier hydrogen bond ͉ histidine ionization constants A histidine tetrad in the pore of the tetrameric M2 protein has long been associated with key channel features of H ϩ selectivity, pH activation, gating, inhibition, and the specific conductance mechanism. M2 protein from influenza A virus conducts protons into the viral core after endocytosis, which leads to the uncoating and release of genetic material into the cytoplasm after fusion of the viral coat with the endosomal wall (1, 2). Much is known about this system from its tetrameric state (2-4), the backbone structure of the transmembrane (TM) domain (5), and numerous electrophysiological (6, 7), biophysical (8-10), and modeling (11) studies that have cast a fascinating tale for this important influenza drug target and the only proton channel of its kind to be characterized in such detail. However, the specific role of His-37 in the tetrameric protein has not been elucidated. Here, we have characterized the pK a s associated with this cluster of four histidine residues in the hydrophobic interstices of the membrane. These pK a values have led us to substantial mechanistic conclusions.There are many lines of evidence, reviewed by Kelly et al. (6), that support the conclusion that M2 is responsible for viral acidification. In vivo ion conductance recordings have shown pH sensitive conductance resulting in rapid acidification of the Xenopus oocytes (12, 13) and mammalian cells (13-15) containing M2 protein.Preparations of purified M2 protein have also been used to show proton conductance in synthetic lipid bilayers (16,17). Singlechannel conductance measurements with membranes containing M2 protein give clear evidence that it is H ϩ conductance, not counterion conductance, that is observed. Furthermore, the channel conductance is unchanged by addition of an excess of NaCl (18). Conductance measurements for the isolated TM domain of M2 protein have als...

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confidence: 99%

Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity

Nishimura

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

245

450

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“…Apart from the dominating electrostatic cationeanion interactions, the pairs uric acid-urate also form NeH … N and NeH … O hydrogen bonds ( Table 3). The N … N distances in these strong hydrogen bonds obtained by solid state DFT structure optimization compare 2.633(7) Å in 9-ethylguanine hemihydrochloride [46], 2.692(4) Å in a supramolecular assembly of phthalimide and 2-guanidinobenzimidazole [47] or to 2.724(4) Å in D,L-histidyl-L, D-histidine pentahydrate [48]. When considering the large DeH … A angles, the NeH … O bonds in the structure belong to stronger hydrogen bonds.…”

Section: Discussionmentioning

confidence: 99%

Ab initio structure determination of kidney stone potassium quadriurate from synchrotron powder diffraction data, a 150 year problem solved

Bazin

Daudon

Elkaı̈m

et al. 2015

Comptes Rendus. Chimie

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a b s t r a c tThe structure of potassium urate, co-crystallized with uric acid K(C 5 H 3 N 4 O 3 )(C 5 H 4 N 4 O 3 ), from human kidney stones, is determined ab initio from synchrotron powder diffraction data, space group P2 1 /c, a ¼ 3.60504(9) Å, b ¼ 19.9293(7) Å, c ¼ 18.4841(6) Å, b ¼ 100.503(2) , Z ¼ 4. Each uric acid molecule is connected to a urate anion through three hydrogen bonds, both molecules are related by a pseudo-inversion center and are randomly distributed in the crystal. Two of the oxygen atoms of the uric acid molecule and two of the urate anions are involved in the potassium coordination forming KO 7 monocapped trigonal prisms sharing their triangular bases, building infinite chains extending along the short a axis. Such a formulation, though controversial, has been claimed to exist since 1862 and named potassium quadriurate. The crystal structure is optimized by energy minimization (DFT) in the solid state, using a hybrid PBE0 functional. The capacity of the urate anion to connect by strong hydrogen bonds to a uric acid molecule has implications concerning the uric acid transport in biological media.

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“…The histidine molecule adopts the sterically least favourable closed conformation, g+, in both the structures (Bhat & Vijayan, 1978;Krause, Baures & Eggleston, 1991), with X I = 58.2 and X 21 = -96.8 ° in u-histidine glycolate and X 1 = 57.2 and X 2~ = -123.5 ° in DL-histidine glycolate (IUPAC-IUB Commission on Biochemical Nomenclature, 1970). The glycolate ion is planar in both the structures, with the hydroxyl group lying in the plane defined by the other four non-H atoms.…”

Section: Molecular Structurementioning

confidence: 99%

X-ray studies on crystalline complexes involving amino acids and peptides. XXX. Structural invariance and optical resolution through interactions with an achiral molecule in the histidine complexes of glycolic acid

Suresh¹,

Vijayan²

1996

Acta Crystallogr Sect B

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The crystals of DL-histidine glycolate and L-histidine glycolate were prepared and analysed as part of an ongoing programme aimed at studying biologically and evolutionarily important interaction and aggregation pattems. Crystallization experiments involving DL-histidine and glycolic acid yielded, in addition to DL-histidine glycolate, a conglomerate containing crystals of L-histidine glycolate and D-histidine glycolate in an unusual process of chiral separation through interaction with an achiral molecule. The crystal structure of oL-histidine glycolate is made up of alternating layers of unlike molecules as in many other binary complexes involving amino acids. The structure of L-histidine glycolate involves packing of columns containing L-histidine molecules and glycolate ions tightly hydrogen bonded to one another. The arrangement is almost identical to that in the structure of L-histidine acetate, thus providing another example for the invariance of certain aggregation patterns with respect to changes in the molecules involved. The observed aggregation of molecules in the chiral complex also appears to provide a structural rationale for chiral separation of histidine in the presence of glycolic acid.

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Histidyl conformations and short N–H^...N hydrogen bonds: Structure of D,L-histidyl-L,D-histidine pentahydrate

Cited by 18 publications

References 18 publications

Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity

Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity

Ab initio structure determination of kidney stone potassium quadriurate from synchrotron powder diffraction data, a 150 year problem solved

X-ray studies on crystalline complexes involving amino acids and peptides. XXX. Structural invariance and optical resolution through interactions with an achiral molecule in the histidine complexes of glycolic acid

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Histidyl conformations and short N–H...N hydrogen bonds: Structure of D,L-histidyl-L,D-histidine pentahydrate

Cited by 18 publications

References 18 publications

Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity

Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity

Ab initio structure determination of kidney stone potassium quadriurate from synchrotron powder diffraction data, a 150 year problem solved

X-ray studies on crystalline complexes involving amino acids and peptides. XXX. Structural invariance and optical resolution through interactions with an achiral molecule in the histidine complexes of glycolic acid

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Histidyl conformations and short N–H^...N hydrogen bonds: Structure of D,L-histidyl-L,D-histidine pentahydrate