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==Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.== | |||
<StructureSection load='1j71' size='340' side='right'caption='[[1j71]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1j71]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J71 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j71 OCA], [https://pdbe.org/1j71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j71 RCSB], [https://www.ebi.ac.uk/pdbsum/1j71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j71 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CARP_CANTR CARP_CANTR] | |||
== 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/j7/1j71_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=1j71 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data. | |||
High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.,Symersky J, Monod M, Foundling SI Biochemistry. 1997 Oct 21;36(42):12700-10. PMID:9335526<ref>PMID:9335526</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1j71" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Pepsin|Pepsin]] | |||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Candida tropicalis]] | [[Category: Candida tropicalis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Unidentified]] | [[Category: Unidentified]] | ||
[[Category: Foundling | [[Category: Foundling SI]] | ||
[[Category: Monod | [[Category: Monod M]] | ||
[[Category: Symersky | [[Category: Symersky J]] | ||
Latest revision as of 07:37, 17 October 2024
Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the secreted aspartic proteinase from Candida tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The classic aspartic proteinase bilobal structure and domain topology is conserved in SAPT, with the substrate binding cleft situated between the two domains. Structural comparisons made with pepsin indicate that insertions and deletions in the primary sequence modify the SAPT structure to create a more spacious substrate binding cleft with altered specificity. An unexpected tetrapeptide has been found to occupy binding sites S1'-S3', and this suggests the order of release of peptide products in the catalytic mechanism of these enzymes. Structural features are considered with regard to previous substrate specificity data. High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.,Symersky J, Monod M, Foundling SI Biochemistry. 1997 Oct 21;36(42):12700-10. PMID:9335526[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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