1fmu: Difference between revisions

Revision as of 13:40, 21 February 2008

STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.

OverviewOverview

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.

About this StructureAbout this Structure

1FMU is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Saccharopepsin, with EC number 3.4.23.25 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 Thu Feb 21 12:40:20 2008

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OCA

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-[[Image:1fmu.gif|left|200px]]<br /><applet load="1fmu" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fmu.gif|left|200px]]<br /><applet load="1fmu" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fmu, resolution 2.70&Aring;" />
 '''STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.'''<br />
 ==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 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.
 ==About this Structure==
-FMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MAN, NAG and NDG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FMU OCA].
+FMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NDG:'>NDG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Saccharopepsin Saccharopepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.25 3.4.23.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMU OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Gustchina, A.]]
 [[Category: Kay, J.]]
-[[Category: Lees, W.E.]]
+[[Category: Lees, W E.]]
 [[Category: Li, M.]]
-[[Category: Phylip, L.H.]]
+[[Category: Phylip, L H.]]
 [[Category: Wlodawer, A.]]
 [[Category: MAN]]
@@ Line 25: / Line 25: @@
 [[Category: proteinase a]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:02:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:20 2008''