1nc3: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1nc3.png|left|200px]] | [[Image:1nc3.png|left|200px]] | ||
{{STRUCTURE_1nc3| PDB=1nc3 | SCENE= }} | {{STRUCTURE_1nc3| PDB=1nc3 | SCENE= }} | ||
===Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with formycin A (FMA)=== | ===Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with formycin A (FMA)=== | ||
{{ABSTRACT_PUBMED_12496243}} | {{ABSTRACT_PUBMED_12496243}} | ||
==About this Structure== | ==About this Structure== | ||
[[1nc3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NC3 OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:012496243</ref><ref group="xtra">PMID:015122881</ref><ref group="xtra">PMID:016109423</ref><references group="xtra"/> | ||
[[Category: Adenosylhomocysteine nucleosidase]] | [[Category: Adenosylhomocysteine nucleosidase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
Line 30: | Line 18: | ||
[[Category: Lee, J E.]] | [[Category: Lee, J E.]] | ||
[[Category: Riscoe, M K.]] | [[Category: Riscoe, M K.]] | ||
[[Category: Hydrolase]] | |||
[[Category: Mixed alpha/beta dimer]] | [[Category: Mixed alpha/beta dimer]] | ||
Revision as of 23:43, 5 December 2012
Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with formycin A (FMA)Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with formycin A (FMA)
Template:ABSTRACT PUBMED 12496243
About this StructureAbout this Structure
1nc3 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Lee JE, Cornell KA, Riscoe MK, Howell PL. Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis. J Biol Chem. 2003 Mar 7;278(10):8761-70. Epub 2002 Dec 20. PMID:12496243 doi:10.1074/jbc.M210836200
- ↑ Lee JE, Settembre EC, Cornell KA, Riscoe MK, Sufrin JR, Ealick SE, Howell PL. Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design. Biochemistry. 2004 May 11;43(18):5159-69. PMID:15122881 doi:http://dx.doi.org/10.1021/bi035492h
- ↑ Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL. Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis. J Mol Biol. 2005 Sep 23;352(3):559-74. PMID:16109423 doi:http://dx.doi.org/10.1016/j.jmb.2005.07.027