|
|
| Line 1: |
Line 1: |
| - | | + | #REDIRECT [[6m9d]] This PDB entry is obsolete and replaced by 6m9d |
| - | ==PSEUDOMONAS SERINE-CARBOXYL PROTEINASE COMPLEXED WITH THE INHIBITOR CHYMOSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)==
| + | |
| - | <StructureSection load='1ke2' size='340' side='right' caption='[[1ke2]], [[Resolution|resolution]] 2.00Å' scene=''>
| + | |
| - | == Structural highlights ==
| + | |
| - | <table><tr><td colspan='2'>[[1ke2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KE2 FirstGlance]. <br>
| + | |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
| + | |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSI:AMINO-(2-IMINO-HEXAHYDRO-PYRIMIDIN-4-YL)-ACETIC+ACID'>CSI</scene>, <scene name='pdbligand=PHA:PHENYLALANINAL'>PHA</scene></td></tr>
| + | |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ga1|1ga1]], [[1ga4|1ga4]], [[1ga6|1ga6]], [[1kdv|1kdv]], [[1kdy|1kdy]], [[1kdz|1kdz]], [[1ke1|1ke1]]</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xanthomonalisin Xanthomonalisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.101 3.4.21.101] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ke2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ke2 OCA], [http://pdbe.org/1ke2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ke2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ke2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ke2 ProSAT]</span></td></tr>
| + | |
| - | </table>
| + | |
| - | == 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/ke/1ke2_consurf.spt"</scriptWhenChecked>
| + | |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ke2 ConSurf].
| + | |
| - | <div style="clear:both"></div>
| + | |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number of inhibitors, have been solved and refined at high- to atomic-level resolution. All of these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, and chymostatin, as well as previously studied iodotyrostatin and pseudo-iodotyrostatin) make covalent bonds to the active site Ser287 through their aldehyde moieties, while their side chains occupy subsites S1-S4 of the enzyme. The mode of binding of the inhibitors is almost identical for their P1 and P2 side chains, while significant differences are observed for P3 and P4 (if present). Kinetic parameters for the binding of these nanomolar inhibitors to PSCP have been established and correlated with the observed mode of binding. The preferences of this enzyme for a larger side chain in P2 as well as Tyr or Phe in P1 are explained by the size, shape, and characteristics of the S2 and S1 regions of the protein structure, respectively. Networks of hydrogen bonds involving glutamic and aspartic acids have been analyzed for the atomic-resolution structure of the native enzyme. PSCP contains a calcium-binding site that consists of Asp328, Asp348, three amide carbonyl groups, and a water molecule, in almost perfect octahedral coordination. The presence of Ca(2+) cation is necessary for the activity of the enzyme.
| + | |
| - | | + | |
| - | Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase.,Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K Biochemistry. 2001 Dec 25;40(51):15602-11. PMID:11747435<ref>PMID:11747435</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 1ke2" style="background-color:#fffaf0;"></div>
| + | |
| - | | + | |
| - | ==See Also==
| + | |
| - | *[[Pepsin|Pepsin]]
| + | |
| - | *[[Proteinase|Proteinase]]
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| - | __TOC__
| + | |
| - | </StructureSection>
| + | |
| - | [[Category: Achromobacter georgiopolitanum]]
| + | |
| - | [[Category: Xanthomonalisin]]
| + | |
| - | [[Category: Dauter, Z]]
| + | |
| - | [[Category: Dunn, B M]]
| + | |
| - | [[Category: Goldfarb, N E]]
| + | |
| - | [[Category: Gustchina, A]]
| + | |
| - | [[Category: Li, M]]
| + | |
| - | [[Category: Oda, K]]
| + | |
| - | [[Category: Oyama, H]]
| + | |
| - | [[Category: Uchida, K]]
| + | |
| - | [[Category: Wlodawer, A]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Serine-carboxyl proteinase]]
| + | |
