3bjk
From Proteopedia
(New page: 200px<br /><applet load="3bjk" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bjk, resolution 1.900Å" /> '''Crystal structure o...) |
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| - | [[Image:3bjk.jpg|left|200px]] | + | [[Image:3bjk.jpg|left|200px]] |
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| - | '''Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase: The Asp44Ala mutant enzyme''' | + | {{Structure |
| + | |PDB= 3bjk |SIZE=350|CAPTION= <scene name='initialview01'>3bjk</scene>, resolution 1.900Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cit+Binding+Site+For+Residue+A+1'>AC1</scene>, <scene name='pdbsite=AC2:Cit+Binding+Site+For+Residue+D+155'>AC2</scene>, <scene name='pdbsite=AC3:Cit+Binding+Site+For+Residue+A+155'>AC3</scene>, <scene name='pdbsite=AC4:Edo+Binding+Site+For+Residue+D+156'>AC4</scene>, <scene name='pdbsite=AC5:Edo+Binding+Site+For+Residue+A+156'>AC5</scene>, <scene name='pdbsite=AC6:Edo+Binding+Site+For+Residue+B+155'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+D+157'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+E+155'>AC8</scene>, <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+A+157'>AC9</scene>, <scene name='pdbsite=BC1:Edo+Binding+Site+For+Residue+D+158'>BC1</scene>, <scene name='pdbsite=BC2:Edo+Binding+Site+For+Residue+C+155'>BC2</scene>, <scene name='pdbsite=BC3:Edo+Binding+Site+For+Residue+D+159'>BC3</scene>, <scene name='pdbsite=BC4:Edo+Binding+Site+For+Residue+A+159'>BC4</scene>, <scene name='pdbsite=BC5:Edo+Binding+Site+For+Residue+F+155'>BC5</scene>, <scene name='pdbsite=BC6:Edo+Binding+Site+For+Residue+B+156'>BC6</scene>, <scene name='pdbsite=BC7:Edo+Binding+Site+For+Residue+E+156'>BC7</scene>, <scene name='pdbsite=BC8:Edo+Binding+Site+For+Residue+C+156'>BC8</scene>, <scene name='pdbsite=BC9:Edo+Binding+Site+For+Residue+A+160'>BC9</scene>, <scene name='pdbsite=CC1:Edo+Binding+Site+For+Residue+D+160'>CC1</scene>, <scene name='pdbsite=CC2:Edo+Binding+Site+For+Residue+D+161'>CC2</scene>, <scene name='pdbsite=CC3:Edo+Binding+Site+For+Residue+E+157'>CC3</scene>, <scene name='pdbsite=CC4:Edo+Binding+Site+For+Residue+A+161'>CC4</scene>, <scene name='pdbsite=CC5:Edo+Binding+Site+For+Residue+B+157'>CC5</scene>, <scene name='pdbsite=CC6:Edo+Binding+Site+For+Residue+E+158'>CC6</scene>, <scene name='pdbsite=CC7:Edo+Binding+Site+For+Residue+D+162'>CC7</scene> and <scene name='pdbsite=CC8:Edo+Binding+Site+For+Residue+B+158'>CC8</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= HI0827 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71421 Haemophilus influenzae Rd KW20]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase: The Asp44Ala mutant enzyme''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3BJK is a [ | + | 3BJK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae_rd_kw20 Haemophilus influenzae rd kw20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BJK OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18260643 18260643] |
[[Category: Haemophilus influenzae rd kw20]] | [[Category: Haemophilus influenzae rd kw20]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: s2f]] | [[Category: s2f]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structure 2 function project]] | [[Category: structure 2 function project]] | ||
| - | [[Category: trimer of | + | [[Category: trimer of dimer]] |
[[Category: ycia]] | [[Category: ycia]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:59:31 2008'' |
Revision as of 16:59, 20 March 2008
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| , resolution 1.900Å | |||||||
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| Sites: | , , , , , , , , , , , , , , , , , , , , , , , , and | ||||||
| Ligands: | and | ||||||
| Gene: | HI0827 (Haemophilus influenzae Rd KW20) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase: The Asp44Ala mutant enzyme
Overview
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.
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
Page seeded by OCA on Thu Mar 20 18:59:31 2008
