1e5k: Difference between revisions

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New page: left|200px<br /> <applet load="1e5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5k, resolution 1.35Å" /> '''CRYSTAL STRUCTURE O...
 
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==About this Structure==
==About this Structure==
1E5K is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with LI and CIT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5K OCA]].  
1E5K is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with LI and CIT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: CI1 and CI2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5K OCA]].  


==Reference==
==Reference==
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[[Category: molybdopterin nucleotidyl-transferase]]
[[Category: molybdopterin nucleotidyl-transferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:55:13 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:51:54 2007''

Revision as of 11:47, 30 October 2007

File:1e5k.gif


1e5k, resolution 1.35Å

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CRYSTAL STRUCTURE OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA (PROTEIN FA) FROM ESCHERICHIA COLI AT NEAR ATOMIC RESOLUTION

OverviewOverview

BACKGROUND: All mononuclear molybdoenzymes bind molybdenum in a complex, with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by, attachment of a GMP group to the terminal phosphate of molybdopterin to, form molybdopterin guanine dinucleotide (MGD). This modification reaction, is required for the functioning of many bacterial molybdoenzymes, including the nitrate reductases, dimethylsulfoxide (DMSO) and, trimethylamine-N-oxide (TMAO) reductases, and formate dehydrogenases. The, GMP attachment step is catalyzed by the cellular enzyme MobA. RESULTS: The, crystal structure of the 21.6 kDa E. coli MobA has been determined by MAD, phasing with selenomethionine-substituted protein and subsequently refined, at 1. ... [(full description)]

About this StructureAbout this Structure

1E5K is a [Single protein] structure of sequence from [Escherichia coli] with LI and CIT as [ligands]. Structure known Active Sites: CI1 and CI2. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution., Stevenson CE, Sargent F, Buchanan G, Palmer T, Lawson DM, Structure. 2000 Nov 15;8(11):1115-25. PMID:11080634

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