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| - | [[Image:2bmh.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2bmh| PDB=2bmh | SCENE= }} | | {{STRUCTURE_2bmh| PDB=2bmh | SCENE= }} |
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| - | '''MODELING PROTEIN-SUBSTRATE INTERACTIONS IN THE HEME DOMAIN OF CYTOCHROME P450BM-3'''
| + | ===MODELING PROTEIN-SUBSTRATE INTERACTIONS IN THE HEME DOMAIN OF CYTOCHROME P450BM-3=== |
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| - | ==Overview==
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| - | The crystal structure of heme domain of the fatty acid monooxygenase, cytochrome P450(BM-3), consisting of residues 1-455 has been independently solved to R = 0.18 at 2.0 A. The crystal form used, space group P2(1) with two molecules per asymmetric unit, is isomorphous with that form with residues 1-471 first described by Boddupalli et al. [Boddupalli, Hasemann, Ravinchandran, Lu, Goldsmith, Deisenhofer & Peterson (1992). Proc. Natl Acad. Sci. USA, 89, 5567-5571] and used by Ravichandran, Boddupalli, Hasemann, Peterson & Deisenhofer [(1993). Science, 261, 731-736] to determine the crystal structure. The substrate-access channel consists of a large, hydrophobic cleft that appears to be the most likely route taken by fatty acid substrates. Attempts to soak crystals in mother liquor containing a variety of fatty acid substrates yielded featureless difference Fouriers even though fatty acid substrates are known to bind with dissociation constants in the micro M range. Modeling substrate-enzyme interactions reveals few contacts between the enzyme and substrate. More detailed modeling was carried out by subjecting both molecules in the asymmetric unit to extensive energy minimization. These studies reveal that the heme-domain active-site cleft can undergo a large conformational change that closes the access channel thereby providing enhanced protein-substrate interactions. These conformational changes are prevented from occurring by intermolecular contacts in the crystal lattice which lock the protein in the 'open' conformation. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15299332}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299332 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15299332}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Li, H.]] | | [[Category: Li, H.]] |
| | [[Category: Poulos, T L.]] | | [[Category: Poulos, T L.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:29:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:40:17 2008'' |
Revision as of 10:40, 27 July 2008
Template:STRUCTURE 2bmh
MODELING PROTEIN-SUBSTRATE INTERACTIONS IN THE HEME DOMAIN OF CYTOCHROME P450BM-3
Template:ABSTRACT PUBMED 15299332
About this Structure
2BMH is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
Reference
Modeling protein-substrate interactions in the heme domain of cytochrome P450(BM-3)., Li H, Poulos TL, Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):21-32. PMID:15299332
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