1fc5
From Proteopedia
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- | [[Image:1fc5.gif|left|200px]] | + | [[Image:1fc5.gif|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN''' | + | {{Structure |
+ | |PDB= 1fc5 |SIZE=350|CAPTION= <scene name='initialview01'>1fc5</scene>, resolution 2.2Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1FC5 is a [ | + | 1FC5 is a [[Single protein]] structure of 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=1FC5 OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11428898 11428898] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: MG]] | [[Category: MG]] | ||
[[Category: bsgi]] | [[Category: bsgi]] | ||
- | [[Category: four | + | [[Category: four module]] |
[[Category: molybdopterin]] | [[Category: molybdopterin]] | ||
[[Category: montreal-kingston bacterial structural genomics initiative]] | [[Category: montreal-kingston bacterial structural genomics initiative]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: with magnesium]] | [[Category: with magnesium]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:07:13 2008'' |
Revision as of 09:07, 20 March 2008
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, resolution 2.2Å | |||||||
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Ligands: | |||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN
Overview
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 Structure
1FC5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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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