1i9c: Difference between revisions
New page: left|200px<br /><applet load="1i9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9c, resolution 1.90Å" /> '''GLUTAMATE MUTASE FRO... |
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[[Image:1i9c.jpg|left|200px]]<br /><applet load="1i9c" size=" | [[Image:1i9c.jpg|left|200px]]<br /><applet load="1i9c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1i9c, resolution 1.90Å" /> | caption="1i9c, resolution 1.90Å" /> | ||
'''GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE'''<br /> | '''GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE'''<br /> | ||
==About this Structure== | ==About this Structure== | ||
1I9C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium] with B12, 5AD, GLU and 3MD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methylaspartate_mutase Methylaspartate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.1 5.4.99.1] Full crystallographic information is available from [http:// | 1I9C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium] with <scene name='pdbligand=B12:'>B12</scene>, <scene name='pdbligand=5AD:'>5AD</scene>, <scene name='pdbligand=GLU:'>GLU</scene> and <scene name='pdbligand=3MD:'>3MD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Methylaspartate_mutase Methylaspartate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.1 5.4.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9C OCA]. | ||
==Reference== | |||
Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Osterreichische Akademie der Wissenschaften (APART fellowship 614), the Osterreichische Fonds zur Forderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Gunter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteins. , Gruber K, Reitzer R, Kratky C, Angew Chem Int Ed Engl. 2001 Sep 17;40(18):3377-3380. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11592143 11592143] | |||
[[Category: Clostridium cochlearium]] | [[Category: Clostridium cochlearium]] | ||
[[Category: Methylaspartate mutase]] | [[Category: Methylaspartate mutase]] | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:24 2008'' | ||
Revision as of 14:09, 21 February 2008
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GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE
About this StructureAbout this Structure
1I9C is a Protein complex structure of sequences from Clostridium cochlearium with , , and as ligands. Active as Methylaspartate mutase, with EC number 5.4.99.1 Full crystallographic information is available from OCA.
ReferenceReference
Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Osterreichische Akademie der Wissenschaften (APART fellowship 614), the Osterreichische Fonds zur Forderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Gunter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteins. , Gruber K, Reitzer R, Kratky C, Angew Chem Int Ed Engl. 2001 Sep 17;40(18):3377-3380. PMID:11592143
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