1n1p

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[[Image:1n1p.gif|left|200px]]
 
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{{Structure
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==ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.4 (STREPTOMYCES SP. SA-COO)==
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|PDB= 1n1p |SIZE=350|CAPTION= <scene name='initialview01'>1n1p</scene>, resolution 0.95&Aring;
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<StructureSection load='1n1p' size='340' side='right'caption='[[1n1p]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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<table><tr><td colspan='2'>[[1n1p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N1P FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.95&#8491;</td></tr>
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|GENE= CHOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1931 Streptomyces sp.])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1p OCA], [https://pdbe.org/1n1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n1p RCSB], [https://www.ebi.ac.uk/pdbsum/1n1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1p ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1b4v|1B4V]], [[1mxt|1MXT]], [[1b8s|1B8S]], [[1cc2|1CC2]], [[1ijh|1IJH]], [[1cbo|1CBO]], [[1n4v|1N4V]], [[1n4w|1N4W]], [[1n4u|1N4U]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1p OCA], [http://www.ebi.ac.uk/pdbsum/1n1p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n1p RCSB]</span>
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== Function ==
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[https://www.uniprot.org/uniprot/CHOD_STRS0 CHOD_STRS0] Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n1/1n1p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n1p ConSurf].
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<div style="clear:both"></div>
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'''ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.4 (STREPTOMYCES SP. SA-COO)'''
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==See Also==
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*[[Cholesterol oxidase|Cholesterol oxidase]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Streptomyces sp]]
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==About this Structure==
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[[Category: Lario PI]]
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1N1P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1P OCA].
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[[Category: Vrielink A]]
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14558826 14558826]
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[[Category: Cholesterol oxidase]]
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[[Category: Single protein]]
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[[Category: Streptomyces sp.]]
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[[Category: Lario, P I.]]
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[[Category: Vrielink, A.]]
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[[Category: atomic resolution]]
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[[Category: flavoenzyme]]
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[[Category: oxidoreductase]]
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[[Category: steroid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:24:07 2008''
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Current revision

ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.4 (STREPTOMYCES SP. SA-COO)

PDB ID 1n1p

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