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2j0p

From Proteopedia

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{{STRUCTURE_2j0p| PDB=2j0p | SCENE= }}
{{STRUCTURE_2j0p| PDB=2j0p | SCENE= }}
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'''STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS'''
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===STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16943192 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16943192}}
==About this Structure==
==About this Structure==
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[[Category: Proteobacteria]]
[[Category: Proteobacteria]]
[[Category: Transport]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:10:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:48:21 2008''

Revision as of 18:48, 28 July 2008

Image:2j0p.png

Template:STRUCTURE 2j0p

STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS

Template:ABSTRACT PUBMED 16943192

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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