1fmx

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[[Image:1fmx.gif|left|200px]]
[[Image:1fmx.gif|left|200px]]
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{{Structure
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|PDB= 1fmx |SIZE=350|CAPTION= <scene name='initialview01'>1fmx</scene>, resolution 2.61&Aring;
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The line below this paragraph, containing "STRUCTURE_1fmx", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1fmx| PDB=1fmx | SCENE= }}
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|RELATEDENTRY=[[1fmu|1FMU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmx OCA], [http://www.ebi.ac.uk/pdbsum/1fmx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fmx RCSB]</span>
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}}
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'''STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21'''
'''STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21'''
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[[Category: Phylip, L H.]]
[[Category: Phylip, L H.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
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[[Category: proteinase some]]
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[[Category: Proteinase some]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:31:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:04 2008''
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Revision as of 13:31, 2 May 2008

Image:1fmx.gif

Template:STRUCTURE 1fmx

STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21


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.

About this Structure

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

Reference

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 Fri May 2 16:31:05 2008

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