1aq6
From Proteopedia
(New page: 200px<br /><applet load="1aq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aq6, resolution 1.95Å" /> '''STRUCTURE OF L-2-HAL...) |
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| - | [[Image:1aq6.jpg|left|200px]]<br /><applet load="1aq6" size=" | + | [[Image:1aq6.jpg|left|200px]]<br /><applet load="1aq6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aq6, resolution 1.95Å" /> | caption="1aq6, resolution 1.95Å" /> | ||
'''STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS'''<br /> | '''STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The L-2-haloacid dehalogenase from the 1,2-dichloroethane degrading | + | The L-2-haloacid dehalogenase from the 1,2-dichloroethane degrading bacterium Xanthobacter autotrophicus GJ10 catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Its crystal structure was solved by the method of multiple isomorphous replacement with incorporation of anomalous scattering information and solvent flattening, and was refined at 1.95-A resolution to an R factor of 21.3%. The three-dimensional structure is similar to that of the homologous L-2-haloacid dehalogenase from Pseudomonas sp. YL (1), but the X. autotrophicus enzyme has an extra dimerization domain, an active site cavity that is completely shielded from the solvent, and a different orientation of several catalytically important amino acid residues. Moreover, under the conditions used, a formate ion is bound in the active site. The position of this substrate-analogue provides valuable information on the reaction mechanism and explains the limited substrate specificity of the Xanthobacter L-2-haloacid dehalogenase. |
==About this Structure== | ==About this Structure== | ||
| - | 1AQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus] with FMT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/(S)-2-haloacid_dehalogenase (S)-2-haloacid dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2] Full crystallographic information is available from [http:// | + | 1AQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus] with <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/(S)-2-haloacid_dehalogenase (S)-2-haloacid dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthobacter autotrophicus]] | [[Category: Xanthobacter autotrophicus]] | ||
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
| - | [[Category: Kalk, K | + | [[Category: Kalk, K H.]] |
| - | [[Category: Ridder, I | + | [[Category: Ridder, I S.]] |
| - | [[Category: Rozeboom, H | + | [[Category: Rozeboom, H J.]] |
[[Category: FMT]] | [[Category: FMT]] | ||
[[Category: l-2-haloacid dehalogenase]] | [[Category: l-2-haloacid dehalogenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:12 2008'' |
Revision as of 09:47, 21 February 2008
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STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS
Overview
The L-2-haloacid dehalogenase from the 1,2-dichloroethane degrading bacterium Xanthobacter autotrophicus GJ10 catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Its crystal structure was solved by the method of multiple isomorphous replacement with incorporation of anomalous scattering information and solvent flattening, and was refined at 1.95-A resolution to an R factor of 21.3%. The three-dimensional structure is similar to that of the homologous L-2-haloacid dehalogenase from Pseudomonas sp. YL (1), but the X. autotrophicus enzyme has an extra dimerization domain, an active site cavity that is completely shielded from the solvent, and a different orientation of several catalytically important amino acid residues. Moreover, under the conditions used, a formate ion is bound in the active site. The position of this substrate-analogue provides valuable information on the reaction mechanism and explains the limited substrate specificity of the Xanthobacter L-2-haloacid dehalogenase.
About this Structure
1AQ6 is a Single protein structure of sequence from Xanthobacter autotrophicus with as ligand. Active as (S)-2-haloacid dehalogenase, with EC number 3.8.1.2 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate., Ridder IS, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW, J Biol Chem. 1997 Dec 26;272(52):33015-22. PMID:9407083
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