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.


1xvv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xvv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xvv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xvv| PDB=1xvv | SCENE= }}
{{STRUCTURE_1xvv| PDB=1xvv | SCENE= }}
-
'''Crystal Structure of CaiB mutant D169A in complex with carnitinyl-CoA'''
+
===Crystal Structure of CaiB mutant D169A in complex with carnitinyl-CoA===
-
==Overview==
+
<!--
-
L-Carnitine (R-[-]-3-hydroxy-4-trimethylaminobutyrate) is found in both eukaryotic and prokaryotic cells and participates in diverse processes including long-chain fatty-acid transport and osmoprotection. The enzyme crotonobetainyl/gamma-butyrobetainyl-CoA:carnitine CoA-transferase (CaiB; E.C. 2.8.3.-) catalyzes the first step in carnitine metabolism, leading to the final product gamma-butyrobetaine. The crystal structures of Escherichia coli apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, have been determined and refined to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The monomer and dimer resemble those of formyl-CoA transferase from Oxalobacter formigenes, as well as E. coli YfdW, a putative type-III CoA transferase of unknown function. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. While the location of cofactor binding is similar in the three proteins, the specific CoA-protein interactions vary somewhat between CaiB, formyl-CoA transferase, and YfdW. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB. The observed carnitinyl-CoA product in crystals of the CaiB Asp169Ala mutant cocrystallized with crotonoyl-CoA and carnitine could result from (i) a catalytic mechanism involving a ternary enzyme-substrate complex, independent of a covalent anhydride intermediate with Asp169, (ii) a spontaneous reaction of the substrates in solution, followed by binding to the enzyme, or (iii) an involvement of another residue substituting functionally for Asp169, such as Glu23.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15823031}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15823031 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15823031}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Carnityl-coa]]
[[Category: Carnityl-coa]]
[[Category: Coa-transferase]]
[[Category: Coa-transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:34:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:09:50 2008''

Revision as of 18:10, 27 July 2008

Image:1xvv.png

Template:STRUCTURE 1xvv

Crystal Structure of CaiB mutant D169A in complex with carnitinyl-CoA

Template:ABSTRACT PUBMED 15823031

About this Structure

1XVV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA., Rangarajan ES, Li Y, Iannuzzi P, Cygler M, Matte A, Biochemistry. 2005 Apr 19;44(15):5728-38. PMID:15823031

Page seeded by OCA on Sun Jul 27 21:09:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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