2d3w
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3w OCA], [http://www.ebi.ac.uk/pdbsum/2d3w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d3w RCSB]</span> | ||
}} | }} | ||
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[[Category: sufc]] | [[Category: sufc]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:59 2008'' |
Revision as of 23:29, 30 March 2008
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, resolution 2.5Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of Escherichia coli SufC, an ATPase compenent of the SUF iron-sulfur cluster assembly machinery
Overview
SufC is an ATPase component of the SUF machinery, which is involved in the biosynthesis of Fe-S clusters. To gain insight into the function of this protein, we have determined the crystal structure of Escherichia coli SufC at 2.5A resolution. Despite the similarity of the overall structure with ABC-ATPases (nucleotide-binding domains of ABC transporters), some key differences were observed. Glu171, an invariant residue involved in ATP hydrolysis, is rotated away from the nucleotide-binding pocket to form a SufC-specific salt bridge with Lys152. Due to this salt bridge, D-loop that follows Glu171 is flipped out to the molecular surface, which may sterically inhibit the formation of an active dimer. Thus, the salt bridge may play a critical role in regulating ATPase activity and preventing wasteful ATP hydrolysis. Furthermore, SufC has a unique Q-loop structure on its surface, which may form a binding site for its partner proteins, SufB and/or SufD.
About this Structure
2D3W is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery., Kitaoka S, Wada K, Hasegawa Y, Minami Y, Fukuyama K, Takahashi Y, FEBS Lett. 2006 Jan 9;580(1):137-43. Epub 2005 Dec 6. PMID:16364320
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