2h5c: Difference between revisions

Revision as of 21:30, 27 July 2008

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File:2h5c.png

Template:STRUCTURE 2h5c

0.82A resolution crystal structure of alpha-lytic protease at pH 50.82A resolution crystal structure of alpha-lytic protease at pH 5

Template:ABSTRACT PUBMED 16834383

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 21:30:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2h5c.gif|left|200px]]
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 {{STRUCTURE_2h5c|  PDB=2h5c  |  SCENE=  }}
-'''0.82A resolution crystal structure of alpha-lytic protease at pH 5'''
+===0.82A resolution crystal structure of alpha-lytic protease at pH 5===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16834383}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16834383 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16834383}}
 ==About this Structure==
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 [[Category: Serine protease]]
 [[Category: Ultra-high resolution]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:53:04 2008''
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