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[[Image:1xk7.gif|left|200px]]
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[[Image:1xk7.png|left|200px]]


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{{STRUCTURE_1xk7|  PDB=1xk7  |  SCENE=  }}  
{{STRUCTURE_1xk7|  PDB=1xk7  |  SCENE=  }}  


'''Crystal Structure- C2 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA transferase (CaiB)'''
===Crystal Structure- C2 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA transferase (CaiB)===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15823031}}


==About this Structure==
==About this Structure==
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[[Category: Montreal-kingston bacterial structural genomics initiative]]
[[Category: Montreal-kingston bacterial structural genomics initiative]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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Revision as of 04:51, 29 July 2008

File:1xk7.png

Template:STRUCTURE 1xk7

Crystal Structure- C2 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA transferase (CaiB)

Template:ABSTRACT PUBMED 15823031

About this Structure

1XK7 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

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