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1ibq

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Revision as of 14:19, 11 September 2015

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

Structural highlights

1ibq is a 2 chain structure with sequence from Aspergillus phoenicis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3app, 4ape, 2apr, 1psn, 1eag, 1mpp
Activity:	Aspergillopepsin I, with EC number 3.4.23.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cho SW, Kim N, Choi MU, Shin W. Structure of aspergillopepsin I from Aspergillus phoenicis: variations of the S1'-S2 subsite in aspartic proteinases. Acta Crystallogr D Biol Crystallogr. 2001 Jul;57(Pt 7):948-56. Epub 2001, Jun 21. PMID:11418762

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ibq"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3app|3app]], [[4ape|4ape]], [[2apr|2apr]], [[1psn|1psn]], [[1eag|1eag]], [[1mpp|1mpp]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=1ibq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ibq RCSB], [http://www.ebi.ac.uk/pdbsum/1ibq PDBsum]</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=1ibq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibq OCA], [http://pdbe.org/1ibq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ibq RCSB], [http://www.ebi.ac.uk/pdbsum/1ibq PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PEPA_ASPSA PEPA_ASPSA]] 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).
+[[http://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).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ibq" style="background-color:#fffaf0;"></div>
 ==See Also==

1ibq

From Proteopedia

Revision as of 14:19, 11 September 2015

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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