1va4
From Proteopedia
(New page: 200px<br /><applet load="1va4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1va4, resolution 1.804Å" /> '''Pseudomonas fluores...) |
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| - | [[Image:1va4.gif|left|200px]]<br /><applet load="1va4" size=" | + | [[Image:1va4.gif|left|200px]]<br /><applet load="1va4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1va4, resolution 1.804Å" /> | caption="1va4, resolution 1.804Å" /> | ||
'''Pseudomonas fluorescens aryl esterase'''<br /> | '''Pseudomonas fluorescens aryl esterase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has | + | The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 A by X-ray diffraction and shows a characteristic alpha/beta-hydrolase fold. In addition to catalyzing the hydrolysis of esters in vitro, PFE also shows low bromoperoxidase activity. PFE shows highest structural similarity, including the active-site environment, to a family of non-heme bacterial haloperoxidases, with an r.m.s. deviation in 271 C(alpha) atoms between PFE and its five closest structural neighbors averaging 0.8 A. PFE has far less similarity (r.m.s. deviation in 218 C(alpha) atoms of 5.0 A) to P. fluorescens carboxyl esterase. PFE favors activated esters with small acyl groups, such as phenyl acetate. The X-ray structure of PFE reveals a significantly occluded active site. In addition, several residues, including Trp28 and Met95, limit the size of the acyl-binding pocket, explaining its preference for small acyl groups. |
==About this Structure== | ==About this Structure== | ||
| - | 1VA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arylesterase Arylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.2 3.1.1.2] Full crystallographic information is available from [http:// | + | 1VA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Arylesterase Arylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.2 3.1.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA4 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cheeseman, J | + | [[Category: Cheeseman, J D.]] |
| - | [[Category: Kazlauskas, R | + | [[Category: Kazlauskas, R J.]] |
[[Category: Park, S.]] | [[Category: Park, S.]] | ||
| - | [[Category: Schrag, J | + | [[Category: Schrag, J D.]] |
[[Category: Tocilj, A.]] | [[Category: Tocilj, A.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: non-cofactor dependent haloperoxidase]] | [[Category: non-cofactor dependent haloperoxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:08 2008'' |
Revision as of 13:33, 21 February 2008
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Pseudomonas fluorescens aryl esterase
Overview
The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 A by X-ray diffraction and shows a characteristic alpha/beta-hydrolase fold. In addition to catalyzing the hydrolysis of esters in vitro, PFE also shows low bromoperoxidase activity. PFE shows highest structural similarity, including the active-site environment, to a family of non-heme bacterial haloperoxidases, with an r.m.s. deviation in 271 C(alpha) atoms between PFE and its five closest structural neighbors averaging 0.8 A. PFE has far less similarity (r.m.s. deviation in 218 C(alpha) atoms of 5.0 A) to P. fluorescens carboxyl esterase. PFE favors activated esters with small acyl groups, such as phenyl acetate. The X-ray structure of PFE reveals a significantly occluded active site. In addition, several residues, including Trp28 and Met95, limit the size of the acyl-binding pocket, explaining its preference for small acyl groups.
About this Structure
1VA4 is a Single protein structure of sequence from Pseudomonas fluorescens with as ligand. Active as Arylesterase, with EC number 3.1.1.2 Full crystallographic information is available from OCA.
Reference
Structure of an aryl esterase from Pseudomonas fluorescens., Cheeseman JD, Tocilj A, Park S, Schrag JD, Kazlauskas RJ, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1237-43. Epub 2004, Jun 22. PMID:15213385
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