2h5c

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{{STRUCTURE_2h5c| PDB=2h5c | SCENE= }}
{{STRUCTURE_2h5c| PDB=2h5c | SCENE= }}
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'''0.82A resolution crystal structure of alpha-lytic protease at pH 5'''
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===0.82A resolution crystal structure of alpha-lytic protease at pH 5===
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==Overview==
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To address questions regarding the mechanism of serine protease catalysis, we have solved two X-ray crystal structures of alpha-lytic protease (alphaLP) that mimic aspects of the transition states: alphaLP at pH 5 (0.82 A resolution) and alphaLP bound to the peptidyl boronic acid inhibitor, MeOSuc-Ala-Ala-Pro-boroVal (0.90 A resolution). Based on these structures, there is no evidence of, or requirement for, histidine-flipping during the acylation step of the reaction. Rather, our data suggests that upon protonation of His57, Ser195 undergoes a conformational change that destabilizes the His57-Ser195 hydrogen bond, preventing the back-reaction. In both structures the His57-Asp102 hydrogen bond in the catalytic triad is a normal ionic hydrogen bond, and not a low-barrier hydrogen bond (LBHB) as previously hypothesized. We propose that the enzyme has evolved a network of relatively short hydrogen bonds that collectively stabilize the transition states. In particular, a short ionic hydrogen bond (SIHB) between His57 Nepsilon2 and the substrate's leaving group may promote forward progression of the TI1-to-acylenzyme reaction. We provide experimental evidence that refutes use of either a short donor-acceptor distance or a downfield 1H chemical shift as sole indicators of a LBHB.
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(as it appears on PubMed at http://www.pubmed.gov), where 16834383 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16834383}}
==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Ultra-high resolution]]
[[Category: Ultra-high resolution]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:53:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:30:23 2008''

Revision as of 18:30, 27 July 2008

Image:2h5c.png

Template:STRUCTURE 2h5c

0.82A resolution crystal structure of alpha-lytic protease at pH 5

Template:ABSTRACT PUBMED 16834383

About this Structure

2H5C is a Single protein structure of sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.

Reference

Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:16834383

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