Domain movement in rabbit muscle adenylate kinase might involve proline isomerization

Sheng, Xiang-Rong; Zhang, H.J; Pan, Xian Ming; Li, X.F; Zhou, Jun

doi:10.1016/s0014-5793(97)00951-4

Cited by 17 publications

(12 citation statements)

References 33 publications

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“…The equilibrium constants calculated from both experiments agree very well and the interconversion free energy ⌬G 0 from N 1 to N 2 is calculated according to Equation 31. A previous study reported that the slow phase fluorescence building can be catalyzed by peptidyl prolyl cis/trans isomerases (28). The calculated free energy ⌬G 0 from N 1 to N 2 is close to that of proline isomerization, giving further evidence that the interconversion of the two forms involves the cis/trans peptidyl prolyl isomerization of proline residue.…”

Section: Discussionsupporting

confidence: 61%

“…The fluorescence intensity of ANS bound to a protein is dependent on the microenvironment of the binding site (32). Experiments wherein AK crystals were soaked with ANS or ATP revealed that ANS or ATP binding occurred only with AK of crystalline form B. ANS occupies the pocket formed between the ␤-sheet, loop 16 -22, helix [23][24][25][26][27][28][29][30], and the C-terminal helix. This pocket was originally assigned to the adenosine moiety of AMP site (12), but has recently been recognized as the ATP site (33,34).…”

Section: Discussionmentioning

confidence: 99%

“…In a previous study from this laboratory (28), it was found that the time course of 8-anilino-1-naphthalenesulfonic acid (ANS) binding to AK was a biphasic process. The burst phase ended in the dead-time of the stopped-flow apparatus (about 15 ms), whereas the slow phase completed in about 10 min.…”

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confidence: 99%

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Evidence for at Least Two Native Forms of Rabbit Muscle Adenylate Kinase in Equilibrium in Aqueous Solution

Zhang

Sheng

Niu

et al. 1998

Journal of Biological Chemistry

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The time course of 8-anilino-1-naphthalenesulfonic acid (ANS) binding to adenylate kinase (AK) is a biphasic process. The burst phase ends in the dead-time of the stopped-flow apparatus (about 15 ms), whereas the slow phase completes in about 10 min. A Job's plot tests of the binding stoichiometry demonstrates that there is one ANS binding site on AK, but only about 70% of the enzyme can rapidly bind with ANS, indicating that the conformation of native AK molecules is not homogeneous. Further kinetic analysis shows that the effects of ANS and substrates concentration on the burst and slow phase fluorescence building agree well with the multiple native forms mechanism. One form (denoted N 1 ) binds with ANS, whereas the other (denoted N 2 ) does not. ANS binding to N 1 results in a burst phase fluorescence increase, followed by the interconversion of N 2 to N 1 , to give the slow phase ANS binding. Under urea denaturation conditions, N 2 is easily perturbed by urea and unfolds completely at low denaturant concentrations, whereas N 1 is relatively resistant to denaturation and unfolds at higher denaturant concentrations. The existence of multiple native forms in solution may shed some light on the interpretation of the enzyme catalytic mechanism.It has been accepted that a globular protein in its native state adopts a single, well defined conformation. However, this concept has been challenged by several reports that some proteins may exist in more than one distinct folded form in equilibrium. Evidence for distinguishing multiple native forms of staphylococcal nuclease has come from electrophoretic and NMR studies (1-6). For calbindin D 9K , evidence of multiple forms came not only from NMR studies, but also from x-ray crystal structure (7,8).Adenylate kinase (AK 1 ; EC 2.7.4.3) catalyzes the phosphoryl transfer reaction: MgATP ϩ AMP i MgADP ϩ ADP (9, 10). The enzyme contains two distinct nucleotide binding sites: the MgATP site, which binds MgATP and MgADP, and the AMP site, which is specific for AMP and uncomplexed ADP. The substrate-induced conformation changes in AK have been the subject of a number of investigations (11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22). Based on the comparison of AK crystal structures representing the enzyme in different ligand forms, apo-form (from pig muscle), enzyme-AMP binary complex (from beef heart mitochondrial matrix), and enzyme-AP 5 A complex (from Escherichia coli), Schulz and co-workers (15, 18) suggested that AK undergoes large structural changes upon substrates binding. These conformational changes can be subdivided into two steps; the first change, corresponding to binding to AMP, only involves the displacement of the small ␣-helical domain (residues 30 -59 in E. coli AK), whereas the second change, occurring with additional binding of substrate ATP, mainly involves the displacement of the LID domain (residues 122-159 in E. coli AK). However, it is not clear whether the enzyme achieves its catalytic conformation only upon substrate binding or whether the above confo...

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Section: Discussionsupporting

confidence: 61%

Section: Discussionmentioning

confidence: 99%

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Evidence for at Least Two Native Forms of Rabbit Muscle Adenylate Kinase in Equilibrium in Aqueous Solution

Zhang

Sheng

Niu

et al. 1998

Journal of Biological Chemistry

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“…For the Ca 2ϩ -free form of a C-type mannose binding protein, addition of equimolar amounts of CypA slightly increased the isomerization rate (57). Using 8-anilino-1-naphthalenesulfonic acid (ANS) binding to probe induced-fit conformational changes associated with ATP binding in rabbit muscle adenylate kinase, Sheng et al showed that CypA accelerates ANS binding (58). In both cases, the biological relevance of prolyl isomerization remains unclear.…”

Section: Catalysis Of Cis͞trans Isomerization By Cyclophilin In a Folmentioning

confidence: 99%

Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A

Bosco

Eisenmesser

Pochapsky

et al. 2002

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

208

211

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Packaging of cyclophilin A (CypA) into HIV-1 virions is essential for efficient replication; however, the reason for this is unknown. Incorporation is mediated through binding to the Gly-89 -Pro-90 peptide bond of the N-terminal domain of HIV-1 capsid (CA N ). Despite the fact that CypA is a peptidyl-prolyl cis͞trans isomerase, catalytic activity on CA N has not been observed previously. We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA N but also catalyzes efficiently the cis͞trans isomerization of the Gly-89 -Pro-90 peptide bond. In addition, conformational changes in CA N distal to the CypA binding loop are observed on CypA binding and catalysis. The results provide experimental evidence for efficient CypA catalysis on a natively folded and biologically relevant protein substrate.

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“…[11][12][13] Furthermore, proline isomerization very often is observed not only to be responsible for the rate-limiting step in folding but, even more interestingly, also to influence enzymatic activity. 14,15 The link between protein folding and activity makes the 22-kDa uridine monophosphate/cytidine monophosphate (UMP/CMP) kinase from Dictyostelium discoideum (UmpK, 194 amino acids) an interesting model protein to study. UmpK belongs to the family of nucleoside monophosphate (NMP) kinases and can be considered as a relatively large singledomain protein.…”

Section: Introductionmentioning

confidence: 99%

The Influence of Proline Isomerization and Off-Pathway Intermediates on the Folding Mechanism of Eukaryotic UMP/CMP Kinase

Lorenz

Reinstein

2008

Journal of Molecular Biology

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Domain movement in rabbit muscle adenylate kinase might involve proline isomerization

Cited by 17 publications

References 33 publications

Evidence for at Least Two Native Forms of Rabbit Muscle Adenylate Kinase in Equilibrium in Aqueous Solution

Evidence for at Least Two Native Forms of Rabbit Muscle Adenylate Kinase in Equilibrium in Aqueous Solution

Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A

The Influence of Proline Isomerization and Off-Pathway Intermediates on the Folding Mechanism of Eukaryotic UMP/CMP Kinase

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