2cn4
From Proteopedia
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|PDB= 2cn4 |SIZE=350|CAPTION= <scene name='initialview01'>2cn4</scene>, resolution 2.30Å | |PDB= 2cn4 |SIZE=350|CAPTION= <scene name='initialview01'>2cn4</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=HEM:Po4+Binding+Site+For+Chain+B'>HEM</scene> | |SITE= <scene name='pdbsite=HEM:Po4+Binding+Site+For+Chain+B'>HEM</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cn4 OCA], [http://www.ebi.ac.uk/pdbsum/2cn4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cn4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Letoffe, S.]] | [[Category: Letoffe, S.]] | ||
[[Category: Wandersman, C.]] | [[Category: Wandersman, C.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: PO4]] | ||
[[Category: dimeric form]] | [[Category: dimeric form]] | ||
[[Category: domain swapping]] | [[Category: domain swapping]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''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 02:23:54 2008'' |
Revision as of 23:23, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF THE SECRETED DIMERIC FORM OF THE HEMOPHORE HASA REVEALS A DOMAIN SWAPPING WITH AN EXCHANGED HEME LIGAND
Overview
To satisfy their iron needs, several Gram-negative bacteria use a heme uptake system involving an extracellular heme-binding protein called hemophore. The function of the hemophore is to acquire free or hemoprotein-bound heme and to transfer it to HasR, its specific outer membrane receptor, by protein-protein interaction. The hemophore HasA secreted by Serratia marcescens, an opportunistic pathogen, was the first to be identified and is now very well characterized. HasA is a monomer that binds one b heme with strong affinity. The heme in HasA is highly exposed to solvent and coordinated by an unusual pair of ligands, a histidine and a tyrosine. Here, we report the identification, the characterization and the X-ray structure of a dimeric form of HasA from S. marcescens: DHasA. We show that both monomeric and dimeric forms are secreted in iron deficient conditions by S. marcescens. The crystal structure of DHasA reveals that it is a domain swapped dimer. The overall structure of each monomeric subunit of DHasA is very similar to that of HasA but formed by parts coming from the two different polypeptide chains, involving one of the heme ligands. Consequently DHasA binds two heme molecules by residues coming from both polypeptide chains. We show here that, while DHasA can bind two heme molecules, it is not able to deliver them to the receptor HasR. However, DHasA can efficiently transfer its heme to the monomeric form that, in turn, delivers it to HasR. We assume that DHasA can function as a heme reservoir in the hemophore system.
About this Structure
2CN4 is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand., Czjzek M, Letoffe S, Wandersman C, Delepierre M, Lecroisey A, Izadi-Pruneyre N, J Mol Biol. 2007 Jan 26;365(4):1176-86. Epub 2006 Oct 25. PMID:17113104
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