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New page: left|200px<br /><applet load="1v29" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v29, resolution 2.6Å" /> '''Crystal structure of ... |
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== | ==Crystal structure of Nitrile hydratase from a thermophile Bacillus smithii== | ||
The crystal structure of the nitrile hydratase (NHase) from Bacillus | <StructureSection load='1v29' size='340' side='right'caption='[[1v29]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1v29]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_smithii Bacillus smithii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V29 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v29 OCA], [https://pdbe.org/1v29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v29 RCSB], [https://www.ebi.ac.uk/pdbsum/1v29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v29 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q84FS5_9BACI Q84FS5_9BACI] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v2/1v29_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1v29 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme. | |||
Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii.,Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142<ref>PMID:14637142</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1v29" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nitrile hydratase|Nitrile hydratase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus smithii]] | [[Category: Bacillus smithii]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Hourai S]] | |||
[[Category: Hourai | [[Category: Miki M]] | ||
[[Category: Miki | [[Category: Mitsuda S]] | ||
[[Category: Mitsuda | [[Category: Takashima Y]] | ||
[[Category: Takashima | [[Category: Yanagi K]] | ||
[[Category: Yanagi | |||
Latest revision as of 02:56, 28 December 2023
Crystal structure of Nitrile hydratase from a thermophile Bacillus smithiiCrystal structure of Nitrile hydratase from a thermophile Bacillus smithii
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the nitrile hydratase (NHase) from Bacillus smithii SC-J05-1 was determined. Our analysis of the structure shows that some residues that seem to be responsible for substrate recognition are different from those of other NHases. In particular, the Phe52 in the beta subunit of NHase from B. smithii covers the metal center partially like a small lid and narrows the active site cleft. It is well known that the NHase from B. smithii especially prefers aliphatic nitriles for its substrate rather than aromatic ones, and we can now infer that the Phe52 residue may play a key role in the substrate specificity for this enzyme. This finding leads us to suggest that substitution of these residues may alter the substrate specificity of the enzyme. Crystal structure of nitrile hydratase from a thermophilic Bacillus smithii.,Hourai S, Miki M, Takashima Y, Mitsuda S, Yanagi K Biochem Biophys Res Commun. 2003 Dec 12;312(2):340-5. PMID:14637142[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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