4ape: Difference between revisions
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[[Image:4ape.jpg|left|200px]] | [[Image:4ape.jpg|left|200px]] | ||
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'''THE ACTIVE SITE OF ASPARTIC PROTEINASES''' | '''THE ACTIVE SITE OF ASPARTIC PROTEINASES''' | ||
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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 | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Sewell, B T.]] | [[Category: Sewell, B T.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:20:57 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 22:20, 4 May 2008
THE ACTIVE SITE OF ASPARTIC PROTEINASES
OverviewOverview
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.
About this StructureAbout 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.
ReferenceReference
The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096 Page seeded by OCA on Sun May 4 22:20:57 2008