This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1j1i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1j1i.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1j1i.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1j1i| PDB=1j1i | SCENE= }}
{{STRUCTURE_1j1i| PDB=1j1i | SCENE= }}
-
'''Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12659866}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12659866 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12659866}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Histidine tagged protein]]
[[Category: Histidine tagged protein]]
[[Category: Meta cleavage product hydrolase]]
[[Category: Meta cleavage product hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:41:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:21:31 2008''

Revision as of 11:21, 1 July 2008

Image:1j1i.png

Template:STRUCTURE 1j1i

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

Template:ABSTRACT PUBMED 12659866

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 Tue Jul 1 14:21:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j1i"
Personal tools