Abstract
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 Å resolution, reveals that the enzyme forms a dimer and each monomer consists of two α/β 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.
| Original language | English |
|---|---|
| Pages (from-to) | 422-426 |
| Number of pages | 5 |
| Journal | Nature Structural Biology |
| Volume | 6 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 1999 May 19 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Structural Biology
- Genetics
Cite this
Structure and mechanism of glutamate racemase from Aquifex pyrophilus. / Hwang, Kwang Yeon; Cho, C. S.; Sang Suk Kim, Suk Kim; Sung, H. C.; Yeon Gyu Yu, Gyu Yu; Cho, Y.
In: Nature Structural Biology, Vol. 6, No. 5, 19.05.1999, p. 422-426.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure and mechanism of glutamate racemase from Aquifex pyrophilus
AU - Hwang, Kwang Yeon
AU - Cho, C. S.
AU - Sang Suk Kim, Suk Kim
AU - Sung, H. C.
AU - Yeon Gyu Yu, Gyu Yu
AU - Cho, Y.
PY - 1999/5/19
Y1 - 1999/5/19
N2 - 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 Å resolution, reveals that the enzyme forms a dimer and each monomer consists of two α/β 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.
AB - 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 Å resolution, reveals that the enzyme forms a dimer and each monomer consists of two α/β 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0032915050&partnerID=8YFLogxK
U2 - 10.1038/8223
DO - 10.1038/8223
M3 - Article
C2 - 10331867
AN - SCOPUS:0032915050
VL - 6
SP - 422
EP - 426
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
SN - 1545-9993
IS - 5
ER -