1ibq

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{{Seed}}
 
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[[Image:1ibq.png|left|200px]]
 
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==ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS==
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The line below this paragraph, containing "STRUCTURE_1ibq", creates the "Structure Box" on the page.
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<StructureSection load='1ibq' size='340' side='right'caption='[[1ibq]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1ibq| PDB=1ibq | SCENE= }}
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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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS===
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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:11418762<ref>PMID:11418762</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ibq" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11418762}}, adds the Publication Abstract to the page
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*[[Pepsin|Pepsin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11418762 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11418762}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1IBQ is a 2 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:11418762</ref><references group="xtra"/>
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[[Category: Aspergillopepsin I]]
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[[Category: Aspergillus phoenicis]]
[[Category: Aspergillus phoenicis]]
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[[Category: Cho, S W.]]
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[[Category: Large Structures]]
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[[Category: Shin, W.]]
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[[Category: Cho SW]]
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[[Category: Aspartic proteinase]]
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[[Category: Shin W]]
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[[Category: Aspergillopepsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 00:25:01 2009''
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Current revision

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

PDB ID 1ibq

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