Structure of d -allose binding protein from Escherichia coli bound to d -allose at 1.8 Å resolution 1 1Edited by A. R. Fersht

Chaudhuri, Barnali N.; Ko, Jong Soo; Park, Chankyu; Jones, T. Alwyn; Mowbray, Sherry L.

doi:10.1006/jmbi.1999.2571

Cited by 55 publications

(47 citation statements)

References 49 publications

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“…All three changes (Ile 20 3 Asp, Glu 27 3 Arg and Ala 103 3 Asn) are clearly observed in the electron density in all structures. In all of the new structures, the electron density also clearly shows an unusual non-proline cis peptide between residues Gly 75 and His 76 that was not noted previously; this does not appear to have any functional significance.…”

Section: Resultsmentioning

confidence: 78%

X-ray Structures of the Leucine-binding Protein Illustrate Conformational Changes and the Basis of Ligand Specificity

Magnusson

Salopek‐Sondi

Luck

et al. 2004

Journal of Biological Chemistry

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The periplasmic leucine-binding protein is the primary receptor for the leucine transport system in Escherichia coli. We report here the structure of an open ligand-free form solved by molecular replacement and refined at 1.5-Å resolution. In addition, two closed ligand-bound structures of the same protein are presented, a phenylalanine-bound form at 1.8 Å and a leucine-bound structure at a nominal resolution of 2.4 Å. These structures show the basis of this protein's ligand specificity, as well as illustrating the conformational changes that are associated with ligand binding. Comparison with earlier structures provides further information about solution conformations, as well as the different specificity of the closely related leucine/ isoleucine/valine-binding protein.

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Section: Resultsmentioning

confidence: 78%

X-ray Structures of the Leucine-binding Protein Illustrate Conformational Changes and the Basis of Ligand Specificity

Magnusson

Salopek‐Sondi

Luck

et al. 2004

Journal of Biological Chemistry

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“…Tp38 contains six Trp residues, at positions 37, 106, 145, 157, 262, and 280 (3). Members of our laboratory previously postulated (3) that Trp-145 is equivalent in importance to Trp-183, which contributes to the binding pocket of E. coli MglB and mediates the hydrophobic contact between the protein and D-glucose or D-galactose (6). To test this hypothesis, we performed site-directed mutagenesis to create a Tp38 mutant protein (W145F) wherein Trp-145 was replaced with Phe.…”

Section: Resultsmentioning

confidence: 99%

“…Whereas analogous receptors of ABC transport systems tend to be heterologous at the primary sequence level, they often possess similarities with respect to the manner in which their binding clefts are configured (6,33,40). In this regard, of the 19 amino acids that form the carbohydrate binding pocket of E. coli MglB (34), Tp38 has identity with 11, including Trp-145, which likely corresponds to the essential Trp-183 in E. coli MglB (3).…”

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confidence: 99%

The Tp38 (TpMglB-2) Lipoprotein Binds Glucose in a Manner Consistent with Receptor Function in Treponema pallidum

et al. 2004

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A 38-kDa lipoprotein of Treponema pallidum (Tp38) was predicted to be a periplasmic sugar-binding protein based on its sequence similarity to the glucose/galactose-binding ( Treponema pallidum, the spirochetal agent of syphilis, continues to be highly enigmatic. Despite the availability of T. pallidum genome sequence information (11), many fundamental aspects of the organism's basic physiology and metabolism remain obscure (30). In this regard, members of our laboratory previously reported that a 38-kDa membrane lipoprotein of T. pallidum (Tp38) was 58.9% similar to the MglB (glucose and galactose binding) proteins of Escherichia coli and Salmonella enterica serovar Typhimurium (3), suggesting that it is a homolog of E. coli MglB (38).

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“…The groove between the two lobes contains the sugar-binding site. We compared the structure of TMBP with known structures of other sugar-binding proteins (arabinose-binding protein, 27 ribose-binding protein, 29 allose-binding protein, 31 glucose/galactose-binding protein, 28 and maltose-binding protein 20 .) The highest similarity of the overall structure is found between TMBP and MBP: 278 C a atoms of both can be superimposed with a root-mean-square deviation (rmsd) of 1.75 A Ê (cutoff at 3.0 A Ê ).…”

Section: Resultsmentioning

confidence: 99%

The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis at 1.85 Å

Diez

Diederichs

Greller

et al. 2001

Journal of Molecular Biology

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We report the crystallization and structure determination at 1.85 A Ê of the extracellular, membrane-anchored trehalose/maltose-binding protein (TMBP) in complex with its substrate trehalose. TMBP is the substrate recognition site of the high-af®nity trehalose/maltose ABC transporter of the hyperthermophilic Archaeon Thermococcus litoralis. In vivo, this protein is anchored to the membrane, presumably via an N-terminal cysteine lipid modi®cation. The crystallized protein was N-terminally truncated, resulting in a soluble protein exhibiting the same binding characteristics as the wild-type protein. The protein shows the characteristic features of a transport-related, substrate-binding protein and is structurally related to the maltose-binding protein (MBP) of Escherichia coli. It consists of two similar lobes, each formed by a parallel b-sheet¯anked by a-helices on both sides. Both are connected by a hinge region consisting of two antiparallel b-strands and an a-helix. As in MBP, the substrate is bound in the cleft between the lobes by hydrogen bonds and hydrophobic interactions. However, compared to maltose binding in MBP, direct hydrogen bonding between the substrate and the protein prevails while apolar contacts are reduced. To elucidate factors contributing to thermostability, we compared TMBP with its mesophilic counterpart MBP and found differences known from similar investigations. Speci®cally, we ®nd helices that are longer than their structurally equivalent counterparts, and fewer internal cavities.

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Structure of d -allose binding protein from Escherichia coli bound to d -allose at 1.8 Å resolution 1 1Edited by A. R. Fersht

Cited by 55 publications

References 49 publications

X-ray Structures of the Leucine-binding Protein Illustrate Conformational Changes and the Basis of Ligand Specificity

X-ray Structures of the Leucine-binding Protein Illustrate Conformational Changes and the Basis of Ligand Specificity

The Tp38 (TpMglB-2) Lipoprotein Binds Glucose in a Manner Consistent with Receptor Function in Treponema pallidum

The crystal structure of a liganded trehalose/maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis at 1.85 Å

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