1b73
From Proteopedia
(New page: 200px<br /><applet load="1b73" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b73, resolution 2.3Å" /> '''GLUTAMATE RACEMASE FR...) |
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| - | [[Image:1b73.jpg|left|200px]]<br /><applet load="1b73" size=" | + | [[Image:1b73.jpg|left|200px]]<br /><applet load="1b73" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b73, resolution 2.3Å" /> | caption="1b73, resolution 2.3Å" /> | ||
'''GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS'''<br /> | '''GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell | + | Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls. The crystal structure of glutamate racemase from Aquifex pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms a dimer and each monomer consists of two alpha/beta fold domains, a unique structure that has not been observed in other racemases or members of an enolase superfamily. A substrate analog, D-glutamine, binds to the deep pocket formed by conserved residues from two monomers. The structural and mutational analyses allow us to propose a mechanism of metal cofactor-independent glutamate racemase in which two cysteine residues are involved in catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1B73 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_pyrophilus Aquifex pyrophilus]. 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:// | + | 1B73 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_pyrophilus Aquifex pyrophilus]. 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=1B73 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Glutamate racemase]] | [[Category: Glutamate racemase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cho, C | + | [[Category: Cho, C S.]] |
[[Category: Cho, Y.]] | [[Category: Cho, Y.]] | ||
| - | [[Category: Hwang, K | + | [[Category: Hwang, K Y.]] |
| - | [[Category: Kim, S | + | [[Category: Kim, S S.]] |
| - | [[Category: Yu, Y | + | [[Category: Yu, Y G.]] |
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: racemase]] | [[Category: racemase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:20 2008'' |
Revision as of 09:52, 21 February 2008
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GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS
Overview
Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls. The crystal structure of glutamate racemase from Aquifex pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms a dimer and each monomer consists of two alpha/beta fold domains, a unique structure that has not been observed in other racemases or members of an enolase superfamily. A substrate analog, D-glutamine, binds to the deep pocket formed by conserved residues from two monomers. The structural and mutational analyses allow us to propose a mechanism of metal cofactor-independent glutamate racemase in which two cysteine residues are involved in catalysis.
About this Structure
1B73 is a Single protein structure of sequence from Aquifex pyrophilus. Active as Glutamate racemase, with EC number 5.1.1.3 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of glutamate racemase from Aquifex pyrophilus., Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y, Nat Struct Biol. 1999 May;6(5):422-6. PMID:10331867
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