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1ibq

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(New page: 200px<br /><applet load="1ibq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ibq, resolution 2.14&Aring;" /> '''ASPERGILLOPEPSIN FRO...)
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[[Image:1ibq.jpg|left|200px]]<br /><applet load="1ibq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ibq, resolution 2.14&Aring;" />
 
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'''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS'''<br />
 
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==Overview==
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==ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS==
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The crystal structure of aspergillopepsin I (AP) from Aspergillus, phoenicis has been determined at 2.18 A resolution and refined to R and, R(free) factors of 21.5 and 26.0%, respectively. AP has the typical two, beta-barrel domain structure of aspartic proteinases. The structures of, the two independent molecules are partly different, exemplifying the, flexible nature of the aspartic proteinase structure. Notably, the 'flap', in one molecule is closer, with a largest separation of 4.0 A, to the, active site than in the other molecule. AP is most structurally homologous, to penicillopepsin (PP) and then to endothiapepsin (EP), which share, sequence identities of 68 and 56%, respectively. However, AP is similar to, EP but differs from PP in the combined S1'-S2 subsite that is delineated, by a flexible psi-loop in the C-terminal domain. The S1' and S2 subsites, are well defined and small in AP, while there is no definite border, between S1' and S2 and the open space for the S2 subsite is larger in PP., Comparison of the structures indicates that the two amino-acid residues, equivalent to Leu295 and Leu297 of AP are the major determining factors in, shaping the S1'-S2 subsite in the fungal aspartic proteinases.
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<StructureSection load='1ibq' size='340' side='right'caption='[[1ibq]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ibq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_phoenicis Aspergillus phoenicis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBQ 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]] 2.14&#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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1ibq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibq OCA], [https://pdbe.org/1ibq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ibq RCSB], [https://www.ebi.ac.uk/pdbsum/1ibq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ibq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PEPA_ASPPH PEPA_ASPPH] Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin (By similarity).
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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/ib/1ibq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ibq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IBQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_phoenicis Aspergillus phoenicis] with MAN and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspergillopepsin_I Aspergillopepsin I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.18 3.4.23.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IBQ OCA].
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*[[Pepsin|Pepsin]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases., Cho SW, Kim N, Choi MU, Shin W, Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):948-56. Epub 2001, Jun 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11418762 11418762]
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[[Category: Aspergillopepsin I]]
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[[Category: Aspergillus phoenicis]]
[[Category: Aspergillus phoenicis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cho, S.W.]]
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[[Category: Cho SW]]
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[[Category: Shin, W.]]
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[[Category: Shin W]]
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[[Category: MAN]]
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[[Category: ZN]]
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[[Category: aspartic proteinase]]
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[[Category: aspergillopepsin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:15:58 2007''
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Current revision

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

PDB ID 1ibq

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