1fc5: Difference between revisions
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|PDB= 1fc5 |SIZE=350|CAPTION= <scene name='initialview01'>1fc5</scene>, resolution 2.2Å | |PDB= 1fc5 |SIZE=350|CAPTION= <scene name='initialview01'>1fc5</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fc5 OCA], [http://www.ebi.ac.uk/pdbsum/1fc5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fc5 RCSB]</span> | |||
}} | }} | ||
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[[Category: Cygler, M.]] | [[Category: Cygler, M.]] | ||
[[Category: Huang, W.]] | [[Category: Huang, W.]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
[[Category: four module]] | [[Category: four module]] | ||
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[[Category: with magnesium]] | [[Category: with magnesium]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:20:04 2008'' | ||
Revision as of 20:20, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
OverviewOverview
MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions.
About this StructureAbout this Structure
1FC5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway., Schrag JD, Huang W, Sivaraman J, Smith C, Plamondon J, Larocque R, Matte A, Cygler M, J Mol Biol. 2001 Jul 6;310(2):419-31. PMID:11428898
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