1j1i
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= CarC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29580 Janthinobacterium]) | |GENE= CarC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29580 Janthinobacterium]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1i OCA], [http://www.ebi.ac.uk/pdbsum/1j1i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j1i RCSB]</span> | ||
}} | }} | ||
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[[Category: meta cleavage product hydrolase]] | [[Category: meta cleavage product hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:36 2008'' |
Revision as of 18:27, 30 March 2008
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| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | CarC (Janthinobacterium) | ||||||
| Activity: | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase, with EC number 3.7.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 21:27:36 2008
Categories: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase | Janthinobacterium | Single protein | Ayabe, Y. | Fushinobu, S. | Habe, H. | Morii, K. | Nam, J W. | Nojiri, H. | Omori, T. | Wakagi, T. | Yamane, H. | Yoshida, T. | Alpha/beta-hydrolase | Aromatic compound | Beta-ketolase | Carbazole degradation | Dibenzofuran | Dioxin | Histidine tagged protein | Meta cleavage product hydrolase
