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4ape
From Proteopedia
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| - | [[Image:4ape.jpg|left|200px]]<br /><applet load="4ape" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="4ape, resolution 2.1Å" /> | ||
| - | '''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''<br /> | ||
| - | == | + | ==THE ACTIVE SITE OF ASPARTIC PROTEINASES== |
| - | The active site of the aspartic proteinase, endothiapepsin, has been | + | <StructureSection load='4ape' size='340' side='right'caption='[[4ape]], [[Resolution|resolution]] 2.10Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ape]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crypa Crypa]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ape 2ape] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ape 1ape]. The December 2000 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Pepsin'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2000_12 10.2210/rcsb_pdb/mom_2000_12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4APE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4APE FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] </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=4ape FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ape OCA], [http://pdbe.org/4ape PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ape RCSB], [http://www.ebi.ac.uk/pdbsum/4ape PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ape 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/ap/4ape_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=4ape ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups. | ||
| - | + | The active site of aspartic proteinases.,Pearl L, Blundell T FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096<ref>PMID:6381096</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 4ape" style="background-color:#fffaf0;"></div> |
| + | |||
| + | ==See Also== | ||
| + | *[[Pepsin|Pepsin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Crypa]] | ||
[[Category: Endothiapepsin]] | [[Category: Endothiapepsin]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pepsin]] | [[Category: Pepsin]] | ||
| - | [[Category: | + | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L]] |
| - | [[Category: Cooper, J | + | [[Category: Cooper, J B]] |
| - | [[Category: Jenkins, J | + | [[Category: Jenkins, J A]] |
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H]] |
| - | [[Category: Sewell, B | + | [[Category: Sewell, B T]] |
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Current revision
THE ACTIVE SITE OF ASPARTIC PROTEINASES
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