1fmu: Difference between revisions

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-{{Seed}}
-[[Image:1fmu.png|left|200px]]
-<!--
+==STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.==
-The line below this paragraph, containing "STRUCTURE_1fmu", creates the "Structure Box" on the page.
+<StructureSection load='1fmu' size='340' side='right'caption='[[1fmu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1fmu]] is a 1 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=1FMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMU FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
-{{STRUCTURE_1fmu|  PDB=1fmu  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fmu OCA], [https://pdbe.org/1fmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fmu RCSB], [https://www.ebi.ac.uk/pdbsum/1fmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fmu ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fmu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1fmu ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===STRUCTURE OF NATIVE PROTEINASE A IN P3221 SPACE GROUP.===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1fmu" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_12127998}}, adds the Publication Abstract to the page
+*[[Pepsin|Pepsin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 12127998 is the PubMed ID number.
+*[[Proteinase 3D structures|Proteinase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_12127998}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-FMU is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMU OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:12127998</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Saccharopepsin]]
+[[Category: Gustchina A]]
-[[Category: Gustchina, A.]]
+[[Category: Kay J]]
-[[Category: Kay, J.]]
+[[Category: Lees WE]]
-[[Category: Lees, W E.]]
+[[Category: Li M]]
-[[Category: Li, M.]]
+[[Category: Phylip LH]]
-[[Category: Phylip, L H.]]
+[[Category: Wlodawer A]]
-[[Category: Wlodawer, A.]]
-[[Category: Proteinase some]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:44:26 2009''