1ibq
From Proteopedia
(New page: 200px<br /><applet load="1ibq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ibq, resolution 2.14Å" /> '''ASPERGILLOPEPSIN FRO...) |
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| - | [[Image:1ibq.jpg|left|200px]]<br /><applet load="1ibq" size=" | + | [[Image:1ibq.jpg|left|200px]]<br /><applet load="1ibq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ibq, resolution 2.14Å" /> | caption="1ibq, resolution 2.14Å" /> | ||
'''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS'''<br /> | '''ASPERGILLOPEPSIN FROM ASPERGILLUS PHOENICIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of aspergillopepsin I (AP) from Aspergillus | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=MAN:'>MAN</scene> and <scene name='pdbligand=ZN:'>ZN</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Aspergillus phoenicis]] | [[Category: Aspergillus phoenicis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cho, S | + | [[Category: Cho, S W.]] |
[[Category: Shin, W.]] | [[Category: Shin, W.]] | ||
[[Category: MAN]] | [[Category: MAN]] | ||
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[[Category: aspergillopepsin]] | [[Category: aspergillopepsin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:14 2008'' |
Revision as of 11:10, 21 February 2008
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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 with and as ligands. Active as Aspergillopepsin I, with EC number 3.4.23.18 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
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