1zuw
From Proteopedia
(New page: 200px<br /><applet load="1zuw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zuw, resolution 1.75Å" /> '''Crystal structure of...) |
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| - | [[Image:1zuw.gif|left|200px]]<br /><applet load="1zuw" size=" | + | [[Image:1zuw.gif|left|200px]]<br /><applet load="1zuw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zuw, resolution 1.75Å" /> | caption="1zuw, resolution 1.75Å" /> | ||
'''Crystal structure of B.subtilis glutamate racemase (RacE) with D-Glu'''<br /> | '''Crystal structure of B.subtilis glutamate racemase (RacE) with D-Glu'''<br /> | ||
==Overview== | ==Overview== | ||
| - | D-glutamate is an essential building block of the peptidoglycan layer in | + | D-glutamate is an essential building block of the peptidoglycan layer in bacterial cell walls and can be synthesized from L-glutamate by glutamate racemase (RacE). The structure of a complex of B. subtilis RacE with D-glutamate reveals that the glutamate is buried in a deep pocket, whose formation at the interface of the enzyme's two domains involves a large-scale conformational rearrangement. These domains are related by pseudo-2-fold symmetry, which superimposes the two catalytic cysteine residues, which are located at equivalent positions on either side of the alpha carbon of the substrate. The structural similarity of these two domains suggests that the racemase activity of RacE arose as a result of gene duplication. The structure of the complex is dramatically different from that proposed previously and provides new insights into the RacE mechanism and an explanation for the potency of a family of RacE inhibitors, which have been developed as novel antibiotics. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with DGL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamate_racemase Glutamate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.3 5.1.1.3] Full crystallographic information is available from [http:// | + | 1ZUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=DGL:'>DGL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamate_racemase Glutamate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.3 5.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Glutamate racemase]] | [[Category: Glutamate racemase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, P | + | [[Category: Baker, P J.]] |
| - | [[Category: Rice, D | + | [[Category: Rice, D W.]] |
| - | [[Category: Ruzheinikov, S | + | [[Category: Ruzheinikov, S N.]] |
| - | [[Category: Sedelnikova, S | + | [[Category: Sedelnikova, S E.]] |
| - | [[Category: Taal, M | + | [[Category: Taal, M A.]] |
[[Category: DGL]] | [[Category: DGL]] | ||
[[Category: glutamate racemase; (r)-glutamate; peptidoglycan biosynthesis]] | [[Category: glutamate racemase; (r)-glutamate; peptidoglycan biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:18 2008'' |
Revision as of 14:19, 21 February 2008
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Crystal structure of B.subtilis glutamate racemase (RacE) with D-Glu
Overview
D-glutamate is an essential building block of the peptidoglycan layer in bacterial cell walls and can be synthesized from L-glutamate by glutamate racemase (RacE). The structure of a complex of B. subtilis RacE with D-glutamate reveals that the glutamate is buried in a deep pocket, whose formation at the interface of the enzyme's two domains involves a large-scale conformational rearrangement. These domains are related by pseudo-2-fold symmetry, which superimposes the two catalytic cysteine residues, which are located at equivalent positions on either side of the alpha carbon of the substrate. The structural similarity of these two domains suggests that the racemase activity of RacE arose as a result of gene duplication. The structure of the complex is dramatically different from that proposed previously and provides new insights into the RacE mechanism and an explanation for the potency of a family of RacE inhibitors, which have been developed as novel antibiotics.
About this Structure
1ZUW is a Single protein structure of sequence from Bacillus subtilis with as ligand. Active as Glutamate racemase, with EC number 5.1.1.3 Full crystallographic information is available from OCA.
Reference
Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery., Ruzheinikov SN, Taal MA, Sedelnikova SE, Baker PJ, Rice DW, Structure. 2005 Nov;13(11):1707-13. PMID:16271894
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