3bjk

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{{STRUCTURE_3bjk| PDB=3bjk | SCENE= }}
{{STRUCTURE_3bjk| PDB=3bjk | SCENE= }}
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'''Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase: The Asp44Ala mutant enzyme'''
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===Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase: The Asp44Ala mutant enzyme===
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==Overview==
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The crystal structure of HI0827 from Haemophilus influenzae Rd KW20, initially annotated "hypothetical protein" in sequence databases, exhibits an acyl-coenzyme A (acyl-CoA) thioesterase "hot dog" fold with a trimer of dimers oligomeric association, a novel assembly for this enzyme family. In studies described in the preceding paper [Zhuang, Z., Song, F., Zhao, H., Li, L., Cao, J., Eisenstein, E., Herzberg, O., and Dunaway-Mariano, D. (2008) Biochemistry 47, XXXX-XXXX], HI0827 is shown to be an acyl-CoA thioesterase that acts on a wide range of acyl-CoA compounds. Two substrate binding sites are located across the dimer interface. The binding sites are occupied by two CoA molecules, one with full occupancy and the second only partially occupied. The CoA molecules, acquired from HI0827-expressing Escherichia coli cells, remained tightly bound to the enzyme through the protein purification steps. The difference in CoA occupancies indicates a different substrate affinity for each of the binding sites, which in turn implies that the enzyme might be subject to allosteric regulation. Mutagenesis studies have shown that the replacement of the putative catalytic carboxylate Asp44 with an alanine residue abolishes activity. The impact of this mutation is seen in the crystal structure of D44A HI0827. Whereas the overall fold and assembly of the mutant protein are the same as those of the wild-type enzyme, the CoA ligands are absent. The dimer interface is perturbed, and the channel that accommodates the thioester acyl chain is more open and wider than that observed in the wild-type enzyme. A model of intact substrate bound to wild-type HI0827 provides a structural rationale for the broad substrate range.
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(as it appears on PubMed at http://www.pubmed.gov), where 18260643 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18260643}}
==About this Structure==
==About this Structure==
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[[Category: Trimer of dimer]]
[[Category: Trimer of dimer]]
[[Category: Ycia]]
[[Category: Ycia]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:36:21 2008''

Revision as of 02:36, 28 July 2008

Image:3bjk.png

Template:STRUCTURE 3bjk

Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase: The Asp44Ala mutant enzyme

Template:ABSTRACT PUBMED 18260643

About this Structure

3BJK is a Single protein structure of sequence from Haemophilus influenzae rd kw20. Full crystallographic information is available from OCA.

Reference

Structure of YciA from Haemophilus influenzae (HI0827), a Hexameric Broad Specificity Acyl-Coenzyme A Thioesterase(,)., Willis MA, Zhuang Z, Song F, Howard A, Dunaway-Mariano D, Herzberg O, Biochemistry. 2008 Feb 9;. PMID:18260643

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