2h8l

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[[Image:2h8l.gif|left|200px]]
[[Image:2h8l.gif|left|200px]]
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{{Structure
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|PDB= 2h8l |SIZE=350|CAPTION= <scene name='initialview01'>2h8l</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_2h8l", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span>
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|GENE= PDIA3, ERP60, GRP58 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2h8l| PDB=2h8l | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h8l OCA], [http://www.ebi.ac.uk/pdbsum/2h8l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h8l RCSB]</span>
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'''Crystal structure of the bb' fragment of ERp57'''
'''Crystal structure of the bb' fragment of ERp57'''
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[[Category: Kozlov, G.]]
[[Category: Kozlov, G.]]
[[Category: Schrag, J D.]]
[[Category: Schrag, J D.]]
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[[Category: thioredoxin-like fold]]
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[[Category: Thioredoxin-like fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:59:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:26:59 2008''
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Revision as of 02:59, 4 May 2008

Image:2h8l.gif

Template:STRUCTURE 2h8l

Crystal structure of the bb' fragment of ERp57


Overview

The synthesis of proteins in the endoplasmic reticulum (ER) is limited by the rate of correct disulfide bond formation. This process is carried out by protein disulfide isomerases, a family of ER proteins which includes general enzymes such as PDI that recognize unfolded proteins and others that are selective for specific proteins or classes. Using small-angle X-ray scattering and X-ray crystallography, we report the structure of a selective isomerase, ERp57, and its interactions with the lectin chaperone calnexin. Using isothermal titration calorimetry and NMR spectroscopy, we show that the b' domain of ERp57 binds calnexin with micromolar affinity through a conserved patch of basic residues. Disruption of this binding site by mutagenesis abrogates folding of RNase B in an in vitro assay. The relative positions of the ERp57 catalytic sites and calnexin binding site suggest that activation by calnexin is due to substrate recruitment rather than a direct stimulation of ERp57 oxidoreductase activity.

About this Structure

2H8L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the bb' domains of the protein disulfide isomerase ERp57., Kozlov G, Maattanen P, Schrag JD, Pollock S, Cygler M, Nagar B, Thomas DY, Gehring K, Structure. 2006 Aug;14(8):1331-9. PMID:16905107 Page seeded by OCA on Sun May 4 05:59:46 2008

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