2j0p: Difference between revisions
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[[Image:2j0p.gif|left|200px]] | [[Image:2j0p.gif|left|200px]] | ||
'''STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS''' | {{Structure | ||
|PDB= 2j0p |SIZE=350|CAPTION= <scene name='initialview01'>2j0p</scene>, resolution 1.70Å | |||
|SITE= <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=12P:DODECAETHYLENE+GLYCOL'>12P</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2J0P is a [ | 2J0P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0P OCA]. | ||
==Reference== | ==Reference== | ||
An induced fit conformational change underlies the binding mechanism of the heme transport proteobacteria-protein HemS., Schneider S, Sharp KH, Barker PD, Paoli M, J Biol Chem. 2006 Oct 27;281(43):32606-10. Epub 2006 Aug 30. PMID:[http:// | An induced fit conformational change underlies the binding mechanism of the heme transport proteobacteria-protein HemS., Schneider S, Sharp KH, Barker PD, Paoli M, J Biol Chem. 2006 Oct 27;281(43):32606-10. Epub 2006 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16943192 16943192] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia enterocolitica]] | [[Category: Yersinia enterocolitica]] | ||
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[[Category: MLI]] | [[Category: MLI]] | ||
[[Category: PEG]] | [[Category: PEG]] | ||
[[Category: conformational | [[Category: conformational change]] | ||
[[Category: haem]] | [[Category: haem]] | ||
[[Category: haem-binding protein]] | [[Category: haem-binding protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
''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 17:35:53 2008'' | ||
Revision as of 15:35, 20 March 2008
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| 2j0p, resolution 1.70Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | HEM, 12P, MLI and PEG | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS
Overview
Bacteria rely on their environment and/or host to acquire iron and have evolved specialized systems to sequester and transport heme. The heme uptake system HemRSTUV is common to proteobacteria, and a major challenge is to understand the molecular mechanism of heme binding and transfer between the protein molecules that underlie this heme transport relay process. In the Gram-negative pathogen Yersinia enterocolitica, the HemRSTUV system culminates with the cytoplasmic recipient HemS, which stores and delivers heme for cellular needs. HemS belongs to a family of proteins essential and unique to proteobacteria. Here we report on the binding mechanism of HemS based on structural data from its apo- and ligand-loaded forms. This heme carrier protein associates with its cargo through a novel, partly preformed binding pocket, formed between a large beta-sheet dome and a three-helix subdomain. In addition to a histidine interacting with the iron, the complex is stabilized by a distal non-coordinating arginine that packs along the porphyrin plane and extensive electrostatic contacts that firmly anchor the heme propionate groups within the protein. Comparison of apo- and ligand-bound HemS crystal structures reveals striking conformational changes that underlie a "heme-induced fit" binding mechanism. Local shifts in amino acid positions combine with global, rigid body-like domain movements, and together, these bring about a switch from an open, apo-form to a closed, bound state. This is the first report in which both liganded and unliganded forms of a heme transport protein are described, thus providing penetrating insights into its mechanism of heme binding and release.
About this Structure
2J0P is a Single protein structure of sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA.
Reference
An induced fit conformational change underlies the binding mechanism of the heme transport proteobacteria-protein HemS., Schneider S, Sharp KH, Barker PD, Paoli M, J Biol Chem. 2006 Oct 27;281(43):32606-10. Epub 2006 Aug 30. PMID:16943192
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