1fmx

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(New page: 200px<br /><applet load="1fmx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmx, resolution 2.61&Aring;" /> '''STRUCTURE OF NATIVE ...)
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[[Image:1fmx.gif|left|200px]]<br /><applet load="1fmx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fmx, resolution 2.61&Aring;" />
 
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'''STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21'''<br />
 
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==Overview==
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==STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21==
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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.
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<StructureSection load='1fmx' size='340' side='right'caption='[[1fmx]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fmx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.61&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmx OCA], [https://pdbe.org/1fmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmx RCSB], [https://www.ebi.ac.uk/pdbsum/1fmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fmx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:12127998</ref>
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1FMX 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1FMX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12127998 12127998]
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</div>
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[[Category: Saccharomyces cerevisiae]]
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<div class="pdbe-citations 1fmx" style="background-color:#fffaf0;"></div>
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[[Category: Saccharopepsin]]
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[[Category: Single protein]]
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[[Category: Gustchina, A.]]
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[[Category: Kay, J.]]
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[[Category: Lees, W.E.]]
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[[Category: Li, M.]]
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[[Category: Phylip, L.H.]]
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[[Category: Wlodawer, A.]]
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[[Category: NAG]]
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[[Category: proteinase a]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:03:04 2007''
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==See Also==
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*[[Pepsin|Pepsin]]
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Gustchina A]]
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[[Category: Kay J]]
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[[Category: Lees WE]]
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[[Category: Li M]]
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[[Category: Phylip LH]]
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[[Category: Wlodawer A]]

Current revision

STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21

PDB ID 1fmx

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