1fmu: Difference between revisions

Revision as of 03:32, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fmu.png

Template:STRUCTURE 1fmu

STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.

Template:ABSTRACT PUBMED 12127998

About this StructureAbout this Structure

1FMU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae., Gustchina A, Li M, Phylip LH, Lees WE, Kay J, Wlodawer A, Biochem Biophys Res Commun. 2002 Jul 26;295(4):1020-6. PMID:12127998

Page seeded by OCA on Tue Jul 1 03:32:03 2008

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

OCA

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-'''STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.'''
+===STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.===
-==Overview==
+<!--
-The structures of the native Saccharomyces cerevisiae proteinase A have been solved by molecular replacement in the monoclinic and trigonal crystal forms and refined at 2.6-2.7A resolution. These structures agree overall with those of other uninhibited aspartic proteinases. However, an unusual orientation for the side chain of Tyr75, a conserved residue on the flexible "flap" that covers the active site and is important for the activity of these enzymes, was found in the trigonal crystals. A similar conformation of Tyr75 occupying the S1 substrate-binding pocket was previously reported only for chymosin (where it was interpreted as representing a "self-inhibited" state of the enzyme), but for no other aspartic proteinases. Since this orientation of Tyr75 has now been seen in the structures of two members of the family of aspartic proteinases, it might indicate that the placement of that residue in the S1 substrate-binding pocket might have some functional significance, analogous to what was seen for self-inhibited structures of serine proteinases.
+The line below this paragraph, {{ABSTRACT_PUBMED_12127998}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12127998 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12127998}}
 ==About this Structure==
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 [[Category: Wlodawer, A.]]
 [[Category: Proteinase some]]
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