1ocm
From Proteopedia
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| - | [[Image:1ocm.gif|left|200px]]<br /><applet load="1ocm" size=" | + | [[Image:1ocm.gif|left|200px]]<br /><applet load="1ocm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ocm, resolution 1.9Å" /> | caption="1ocm, resolution 1.9Å" /> | ||
'''THE CRYSTAL STRUCTURE OF MALONAMIDASE E2 COVALENTLY COMPLEXED WITH PYROPHOSPHATE FROM BRADYRHIZOBIUM JAPONICUM'''<br /> | '''THE CRYSTAL STRUCTURE OF MALONAMIDASE E2 COVALENTLY COMPLEXED WITH PYROPHOSPHATE FROM BRADYRHIZOBIUM JAPONICUM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OCM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with POP as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1GRK. Known structural/functional Site: <scene name='pdbsite=PP1:Pop Binding Site For Chain B'>PP1</scene>. Full crystallographic information is available from [http:// | + | 1OCM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with <scene name='pdbligand=POP:'>POP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1GRK. Known structural/functional Site: <scene name='pdbsite=PP1:Pop+Binding+Site+For+Chain+B'>PP1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: malonamidase]] | [[Category: malonamidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:10 2008'' |
Revision as of 07:56, 3 February 2008
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THE CRYSTAL STRUCTURE OF MALONAMIDASE E2 COVALENTLY COMPLEXED WITH PYROPHOSPHATE FROM BRADYRHIZOBIUM JAPONICUM
Overview
A large group of hydrolytic enzymes, which contain a conserved stretch of, approximately 130 amino acids designated the amidase signature (AS), sequence, constitutes a super family that is distinct from any other known, hydrolase family. AS family enzymes are widespread in nature, ranging from, bacteria to humans, and exhibit a variety of biological functions. Here we, report the first structure of an AS family enzyme provided by the crystal, structure of malonamidase E2 from Bradyrhizobium japonicum. The structure, representing a new protein fold, reveals a previously unidentified, Ser-cisSer-Lys catalytic machinery that is absolutely conserved throughout, the family. This family of enzymes appears to be evolutionarily distinct, but has diverged to acquire a wide spectrum of individual substrate, specificities, while maintaining a core structure that supports the, catalytic function of the unique triad. Based of the structures of the, enzyme in two different inhibited states, an unusual action mechanism of, the triad is proposed that accounts for the role of the cis conformation, in the triad.
About this Structure
1OCM is a Single protein structure of sequence from Bradyrhizobium japonicum with as ligand. This structure superseeds the now removed PDB entry 1GRK. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature., Shin S, Lee TH, Ha NC, Koo HM, Kim SY, Lee HS, Kim YS, Oh BH, EMBO J. 2002 Jun 3;21(11):2509-16. PMID:12032064
Page seeded by OCA on Sun Feb 3 09:56:10 2008
Categories: Bradyrhizobium japonicum | Single protein | Ha, N.C. | Lee, T.H. | Oh, B.H. | Shin, S. | POP | Amidase | Malonamidase
