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2j0p

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[[Image:2j0p.gif|left|200px]]<br /><applet load="2j0p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2j0p.gif|left|200px]]
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caption="2j0p, resolution 1.70&Aring;" />
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'''STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS'''<br />
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{{Structure
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|PDB= 2j0p |SIZE=350|CAPTION= <scene name='initialview01'>2j0p</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene>
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|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>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF THE HAEM-CHAPERONE PROTEOBACTERIA-PROTEIN HEMS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2J0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=12P:'>12P</scene>, <scene name='pdbligand=MLI:'>MLI</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0P OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16943192 16943192]
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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]]
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[[Category: conformational changes]]
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[[Category: conformational change]]
[[Category: haem]]
[[Category: haem]]
[[Category: haem-binding protein]]
[[Category: haem-binding protein]]
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:06 2008''
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''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

Image:2j0p.gif


PDB ID 2j0p

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands: , , and
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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