1j1i

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[[Image:1j1i.gif|left|200px]]<br /><applet load="1j1i" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j1i.gif|left|200px]]
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caption="1j1i, resolution 1.86&Aring;" />
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'''Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)'''<br />
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{{Structure
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|PDB= 1j1i |SIZE=350|CAPTION= <scene name='initialview01'>1j1i</scene>, resolution 1.86&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/2,6-dioxo-6-phenylhexa-3-enoate_hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.8 3.7.1.8]
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|GENE= CarC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29580 Janthinobacterium])
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}}
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'''Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1J1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Janthinobacterium Janthinobacterium]. Active as [http://en.wikipedia.org/wiki/2,6-dioxo-6-phenylhexa-3-enoate_hydrolase 2,6-dioxo-6-phenylhexa-3-enoate hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.8 3.7.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1I OCA].
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1J1I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Janthinobacterium Janthinobacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1I OCA].
==Reference==
==Reference==
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Crystal structure of a histidine-tagged serine hydrolase involved in the carbazole degradation (CarC enzyme)., Habe H, Morii K, Fushinobu S, Nam JW, Ayabe Y, Yoshida T, Wakagi T, Yamane H, Nojiri H, Omori T, Biochem Biophys Res Commun. 2003 Apr 4;303(2):631-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12659866 12659866]
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Crystal structure of a histidine-tagged serine hydrolase involved in the carbazole degradation (CarC enzyme)., Habe H, Morii K, Fushinobu S, Nam JW, Ayabe Y, Yoshida T, Wakagi T, Yamane H, Nojiri H, Omori T, Biochem Biophys Res Commun. 2003 Apr 4;303(2):631-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12659866 12659866]
[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]
[[Category: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase]]
[[Category: Janthinobacterium]]
[[Category: Janthinobacterium]]
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[[Category: Yoshida, T.]]
[[Category: Yoshida, T.]]
[[Category: alpha/beta-hydrolase]]
[[Category: alpha/beta-hydrolase]]
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[[Category: aromatic compounds]]
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[[Category: aromatic compound]]
[[Category: beta-ketolase]]
[[Category: beta-ketolase]]
[[Category: carbazole degradation]]
[[Category: carbazole degradation]]
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[[Category: meta cleavage product hydrolase]]
[[Category: meta cleavage product hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:45 2008''

Revision as of 09:57, 20 March 2008


PDB ID 1j1i

Drag the structure with the mouse to rotate
, resolution 1.86Å
Gene: CarC (Janthinobacterium)
Activity: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase, with EC number 3.7.1.8
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)


Overview

2-Hydroxy-6-oxo-6-(2(')-aminophenyl)-hexa-2,4-dienoate hydrolases (CarC enzymes) from two carbazole-degrading bacteria were purified using recombinant Escherichia coli strains with the histidine (His)-tagged purification system. The His-tagged CarC (ht-CarC) enzymes from Pseudomonas resinovorans strain CA10 (ht-CarC(CA10)) and Janthinobacterium sp. strain J3 (ht-CarC(J3)) exhibited hydrolase activity toward 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate as the purified native CarC(CA10) did. ht-CarC(J3) was crystallized in the space group I422 with cell dimensions of a=b=130.3A, c=84.5A in the hexagonal setting, and the crystal structure of ht-CarC(J3) was determined at 1.86A resolution. The final refined model of ht-CarC(J3) yields an R-factor of 21.6%, although the electron-density corresponding to Ile146 to Asn155 was ambiguous in the final model. We compared the known structures of BphD from Rhodococcus sp. strain RHA1 and CumD from Pseudomonas fluorescens strain IP01. The backbone conformation of ht-CarC(J3) was better superimposed with CumD than with BphD(RHA1). The side-chain directions of Arg185 and Trp262 residues in the substrate binding pockets of these enzymes were different among these proteins, suggesting that these residues may take a conformational change during the catalytic cycles.

About this Structure

1J1I is a Single protein structure of sequence from Janthinobacterium. Full crystallographic information is available from OCA.

Reference

Crystal structure of a histidine-tagged serine hydrolase involved in the carbazole degradation (CarC enzyme)., Habe H, Morii K, Fushinobu S, Nam JW, Ayabe Y, Yoshida T, Wakagi T, Yamane H, Nojiri H, Omori T, Biochem Biophys Res Commun. 2003 Apr 4;303(2):631-9. PMID:12659866

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