We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2q2o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2q2o.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2q2o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2q2o| PDB=2q2o | SCENE= }}
{{STRUCTURE_2q2o| PDB=2q2o | SCENE= }}
-
'''Crystal structure of H183C Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride'''
+
===Crystal structure of H183C Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride===
-
==Overview==
+
<!--
-
The specific insertion of a divalent metal ion into tetrapyrrole macrocycles is catalyzed by a group of enzymes called chelatases. Distortion of the tetrapyrrole has been proposed to be an important component of the mechanism of metallation. We present the structures of two different inhibitor complexes: (1) N-methylmesoporphyrin (N-MeMP) with the His183Ala variant of Bacillus subtilis ferrochelatase; (2) the wild-type form of the same enzyme with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride (dSDP). Analysis of the structures showed that only one N-MeMP isomer out of the eight possible was bound to the protein and it was different from the isomer that was earlier found to bind to the wild-type enzyme. A comparison of the distortion of this porphyrin with other porphyrin complexes of ferrochelatase and a catalytic antibody with ferrochelatase activity using normal-coordinate structural decomposition reveals that certain types of distortion are predominant in all these complexes. On the other hand, dSDP, which binds closer to the protein surface compared to N-MeMP, does not undergo any distortion upon binding to the protein, underscoring that the position of the porphyrin within the active site pocket is crucial for generating the distortion required for metal insertion. In addition, in contrast to the wild-type enzyme, Cu(2+)-soaking of the His183Ala variant complex did not show any traces of porphyrin metallation. Collectively, these results provide new insights into the role of the active site residues of ferrochelatase in controlling stereospecificity, distortion and metallation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18423489}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18423489 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18423489}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Pi-helix]]
[[Category: Pi-helix]]
[[Category: Rossman fold]]
[[Category: Rossman fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:03:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:54:41 2008''

Revision as of 22:54, 27 July 2008

Image:2q2o.png

Template:STRUCTURE 2q2o

Crystal structure of H183C Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride

Template:ABSTRACT PUBMED 18423489

About this Structure

2Q2O is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues., Karlberg T, Hansson MD, Yengo RK, Johansson R, Thorvaldsen HO, Ferreira GC, Hansson M, Al-Karadaghi S, J Mol Biol. 2008 May 16;378(5):1074-83. Epub 2008 Mar 28. PMID:18423489

Page seeded by OCA on Mon Jul 28 01:54:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q2o"
Personal tools