1ibq

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[[Image:1ibq.jpg|left|200px]]
[[Image:1ibq.jpg|left|200px]]
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{{Structure
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|PDB= 1ibq |SIZE=350|CAPTION= <scene name='initialview01'>1ibq</scene>, resolution 2.14&Aring;
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The line below this paragraph, containing "STRUCTURE_1ibq", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ibq| PDB=1ibq | SCENE= }}
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|RELATEDENTRY=[[3app|3APP]], [[4ape|4APE]], [[2apr|2APR]], [[1psn|1PSN]], [[1eag|1EAG]], [[1mpp|1MPP]]
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1ibq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ibq RCSB]</span>
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}}
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'''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS'''
'''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS'''
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[[Category: Cho, S W.]]
[[Category: Cho, S W.]]
[[Category: Shin, W.]]
[[Category: Shin, W.]]
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[[Category: aspartic proteinase]]
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[[Category: Aspartic proteinase]]
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[[Category: aspergillopepsin]]
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[[Category: Aspergillopepsin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:49:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:29 2008''
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Revision as of 16:49, 2 May 2008

Template:STRUCTURE 1ibq

ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS


Overview

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.

About this Structure

1IBQ is a Single protein structure of sequence from Aspergillus phoenicis. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 19:49:01 2008

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