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1xk6

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{{STRUCTURE_1xk6| PDB=1xk6 | SCENE= }}
{{STRUCTURE_1xk6| PDB=1xk6 | SCENE= }}
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'''Crystal Structure- P1 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA Transferase (CaiB)'''
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===Crystal Structure- P1 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA Transferase (CaiB)===
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==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: Coa transferase]]
[[Category: Coa transferase]]
[[Category: Crotonobetainyl coa]]
[[Category: Crotonobetainyl coa]]
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Revision as of 23:26, 28 July 2008

Image:1xk6.png

Template:STRUCTURE 1xk6

Crystal Structure- P1 form- of Escherichia coli Crotonobetainyl-CoA: carnitine CoA Transferase (CaiB)

Template:ABSTRACT PUBMED 15823031

About this Structure

1XK6 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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