2c7x

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[[Image:2c7x.gif|left|200px]]<br /><applet load="2c7x" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c7x.gif|left|200px]]
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caption="2c7x, resolution 1.75&Aring;" />
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'''CRYSTAL STRUCTURE OF NARBOMYCIN-BOUND CYTOCHROME P450 PIKC (CYP107L1)'''<br />
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{{Structure
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|PDB= 2c7x |SIZE=350|CAPTION= <scene name='initialview01'>2c7x</scene>, resolution 1.75&Aring;
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|SITE= <scene name='pdbsite=AC1:Nrb+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NRB:NARBOMYCIN'>NRB</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF NARBOMYCIN-BOUND CYTOCHROME P450 PIKC (CYP107L1)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NRB:'>NRB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Nrb+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7X OCA].
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2C7X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7X OCA].
==Reference==
==Reference==
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The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae., Sherman DH, Li S, Yermalitskaya LV, Kim Y, Smith JA, Waterman MR, Podust LM, J Biol Chem. 2006 Sep 8;281(36):26289-97. Epub 2006 Jul 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16825192 16825192]
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The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae., Sherman DH, Li S, Yermalitskaya LV, Kim Y, Smith JA, Waterman MR, Podust LM, J Biol Chem. 2006 Sep 8;281(36):26289-97. Epub 2006 Jul 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16825192 16825192]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces venezuelae]]
[[Category: Streptomyces venezuelae]]
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[[Category: pikc]]
[[Category: pikc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:01 2008''

Revision as of 14:12, 20 March 2008

Image:2c7x.gif


PDB ID 2c7x

Drag the structure with the mouse to rotate
, resolution 1.75Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF NARBOMYCIN-BOUND CYTOCHROME P450 PIKC (CYP107L1)


Overview

The pikromycin (Pik)/methymycin biosynthetic pathway of Streptomyces venezuelae represents a valuable system for dissecting the fundamental mechanisms of modular polyketide biosynthesis, aminodeoxysugar assembly, glycosyltransfer, and hydroxylation leading to the production of a series of macrolide antibiotics, including the natural ketolides narbomycin and pikromycin. In this study, we describe four x-ray crystal structures and allied functional studies for PikC, the remarkable P450 monooxygenase responsible for production of a number of related macrolide products from the Pik pathway. The results provide important new insights into the structural basis for the C10/C12 and C12/C14 hydroxylation patterns for the 12-(YC-17) and 14-membered ring (narbomycin) macrolides, respectively. This includes two different ligand-free structures in an asymmetric unit (resolution 2.1 A) and two co-crystal structures with bound endogenous substrates YC-17 (resolution 2.35 A)or narbomycin (resolution 1.7 A). A central feature of the enzyme-substrate interaction involves anchoring of the desosamine residue in two alternative binding pockets based on a series of distinct amino acid residues that form a salt bridge and a hydrogen-bonding network with the deoxysugar C3' dimethylamino group. Functional significance of the salt bridge was corroborated by site-directed mutagenesis that revealed a key role for Glu-94 in YC-17 binding and Glu-85 for narbomycin binding. Taken together, the x-ray structure analysis, site-directed mutagenesis, and corresponding product distribution studies reveal that PikC substrate tolerance and product diversity result from a combination of alternative anchoring modes rather than an induced fit mechanism.

About this Structure

2C7X is a Single protein structure of sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA.

Reference

The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae., Sherman DH, Li S, Yermalitskaya LV, Kim Y, Smith JA, Waterman MR, Podust LM, J Biol Chem. 2006 Sep 8;281(36):26289-97. Epub 2006 Jul 6. PMID:16825192

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