1n3u: Difference between revisions

Revision as of 14:50, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n3u.png

Template:STRUCTURE 1n3u

Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form BCrystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B

Template:ABSTRACT PUBMED 12500973

About this StructureAbout this Structure

1N3U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1., Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, Ortiz de Montellano PR, Poulos TL, J Biol Chem. 2003 Mar 7;278(10):7834-43. Epub 2002 Dec 24. PMID:12500973

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-[[Image:1n3u.gif|left|200px]]
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-'''Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B'''
+===Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B===
-==Overview==
+<!--
-Heme oxygenase (HO) catalyzes the degradation of heme to biliverdin. The crystal structure of human HO-1 in complex with heme reveals a novel helical structure with conserved glycines in the distal helix, providing flexibility to accommodate substrate binding and product release (Schuller, D. J., Wilks, A., Ortiz de Montellano, P. R., and Poulos, T. L. (1999) Nat. Struct. Biol. 6, 860-867). To structurally understand the HO catalytic pathway in more detail, we have determined the crystal structure of human apo-HO-1 at 2.1 A and a higher resolution structure of human HO-1 in complex with heme at 1.5 A. Although the 1.5-A heme.HO-1 model confirms our initial analysis based on the 2.08-A model, the higher resolution structure has revealed important new details such as a solvent H-bonded network in the active site that may be important for catalysis. Because of the absence of the heme, the distal and proximal helices that bracket the heme plane in the holo structure move farther apart in the apo structure, thus increasing the size of the active-site pocket. Nevertheless, the relative positioning and conformation of critical catalytic residues remain unchanged in the apo structure compared with the holo structure, but an important solvent H-bonded network is missing in the apoenzyme. It thus appears that the binding of heme and a tightening of the structure around the heme stabilize the solvent H-bonded network required for proper catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12500973}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12500973 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12500973}}
 ==About this Structure==
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 [[Category: Alpha helice]]
 [[Category: Heme-binding site]]
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