1n1p
From Proteopedia
(New page: 200px<br /><applet load="1n1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n1p, resolution 0.95Å" /> '''ATOMIC RESOLUTION ST...) |
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| - | [[Image:1n1p.gif|left|200px]]<br /><applet load="1n1p" size=" | + | [[Image:1n1p.gif|left|200px]]<br /><applet load="1n1p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n1p, resolution 0.95Å" /> | caption="1n1p, resolution 0.95Å" /> | ||
'''ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.4 (STREPTOMYCES SP. SA-COO)'''<br /> | '''ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.4 (STREPTOMYCES SP. SA-COO)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of the flavoenzyme cholesterol oxidase, SCOA | + | The X-ray crystal structure of the flavoenzyme cholesterol oxidase, SCOA (Streptomyces sp.SA-COO) has been determined to 0.95 A resolution. The large size (55kDa) and the high-resolution diffraction of this protein provides a unique opportunity to observe detailed electronic effects within a protein environment and to obtain a larger sampling for which to analyze these electronic and structural differences. It is well-known through spectroscopic methods that peptide carbonyl groups are polarized in alpha-helices. This electronic characteristic is evident in the sub-Angstrom electron density of SCOA. Our analysis indicates an increased tendency for the electron density of the main chain carbonyl groups within alpha-helices to be polarized toward the oxygen atoms. In contrast, the carbonyl groups in beta-sheet structures tend to exhibit a greater charge density between the carbon and oxygen atoms. Interestingly, the electronic differences observed at the carbonyl groups do not appear to be correlated to the bond distance of the peptide bond or the peptide planarity. This study gives important insight into the electronic effects of alpha-helix dipoles in enzymes and provides experimentally based observations that have not been previously characterized in protein structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1N1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with MN, FAD and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6] Full crystallographic information is available from [http:// | + | 1N1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
| - | [[Category: Lario, P | + | [[Category: Lario, P I.]] |
[[Category: Vrielink, A.]] | [[Category: Vrielink, A.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: steroid metabolism]] | [[Category: steroid metabolism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:17 2008'' |
Revision as of 12:01, 21 February 2008
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ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.4 (STREPTOMYCES SP. SA-COO)
Overview
The X-ray crystal structure of the flavoenzyme cholesterol oxidase, SCOA (Streptomyces sp.SA-COO) has been determined to 0.95 A resolution. The large size (55kDa) and the high-resolution diffraction of this protein provides a unique opportunity to observe detailed electronic effects within a protein environment and to obtain a larger sampling for which to analyze these electronic and structural differences. It is well-known through spectroscopic methods that peptide carbonyl groups are polarized in alpha-helices. This electronic characteristic is evident in the sub-Angstrom electron density of SCOA. Our analysis indicates an increased tendency for the electron density of the main chain carbonyl groups within alpha-helices to be polarized toward the oxygen atoms. In contrast, the carbonyl groups in beta-sheet structures tend to exhibit a greater charge density between the carbon and oxygen atoms. Interestingly, the electronic differences observed at the carbonyl groups do not appear to be correlated to the bond distance of the peptide bond or the peptide planarity. This study gives important insight into the electronic effects of alpha-helix dipoles in enzymes and provides experimentally based observations that have not been previously characterized in protein structure.
About this Structure
1N1P is a Single protein structure of sequence from Streptomyces sp. with , and as ligands. Active as Cholesterol oxidase, with EC number 1.1.3.6 Full crystallographic information is available from OCA.
Reference
Atomic resolution density maps reveal secondary structure dependent differences in electronic distribution., Lario PI, Vrielink A, J Am Chem Soc. 2003 Oct 22;125(42):12787-94. PMID:14558826
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