4ape

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[[Image:4ape.jpg|left|200px]]
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==Overview==
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{{ABSTRACT_6381096}}
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The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.
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==About this Structure==
==About this Structure==
4APE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ape 1ape]. The following page contains interesting information on the relation of 4APE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb12_1.html Pepsin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4APE OCA].
4APE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. This structure supersedes the now removed PDB entries and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ape 1ape]. The following page contains interesting information on the relation of 4APE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb12_1.html Pepsin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4APE OCA].
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==Reference==
 
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The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6381096 6381096]
 
[[Category: Cryphonectria parasitica]]
[[Category: Cryphonectria parasitica]]
[[Category: Endothiapepsin]]
[[Category: Endothiapepsin]]
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[[Category: Pearl, L H.]]
[[Category: Pearl, L H.]]
[[Category: Sewell, B T.]]
[[Category: Sewell, B T.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:20:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:28:37 2008''

Revision as of 15:28, 26 June 2008

Image:4ape.png

Template:STRUCTURE 4ape

THE ACTIVE SITE OF ASPARTIC PROTEINASES


Template:ABSTRACT 6381096

About this Structure

4APE is a Single protein structure of sequence from Cryphonectria parasitica. This structure supersedes the now removed PDB entries and 1ape. The following page contains interesting information on the relation of 4APE with [Pepsin]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 18:28:37 2008

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