2zcf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:51, 9 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2zcf.gif|left|200px]]
 
-
<!--
+
==Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771==
-
The line below this paragraph, containing "STRUCTURE_2zcf", creates the "Structure Box" on the page.
+
<StructureSection load='2zcf' size='340' side='right'caption='[[2zcf]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2zcf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZCF FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.43&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-
{{STRUCTURE_2zcf| PDB=2zcf | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcf OCA], [https://pdbe.org/2zcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zcf RCSB], [https://www.ebi.ac.uk/pdbsum/2zcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zcf ProSAT], [https://www.topsan.org/Proteins/RSGI/2zcf TOPSAN]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NHAA_RHOER NHAA_RHOER] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class.
 +
== 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/zc/2zcf_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2zcf ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic center, with glutamic acid or asparagine. The kcat of alphaQ90E and alphaQ90N mutants decreased to 24% and 5% that of wild type respectively, but the effect of mutations on Km was not very significant. In both mutants, the alphaCys114-SOH modification appeared to be responsible for the catalysis as in native NHase. We crystallized the nitrosylated alphaQ90N mutant and determined its structure at a resolution of 1.43 A. The structure was basically identical to that of native nitrosylated NHase except for the mutated site and its vicinity. The structural difference between native and alphaQ90N mutant NHases suggested the importance of the hydrogen bond networks between alphaGln90 and the iron center for the catalytic activity.
-
'''Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771'''
+
Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771.,Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:16636455<ref>PMID:16636455</ref>
-
 
+
-
 
+
-
==Overview==
+
-
Nitrile hydratase (NHase) from Rhodococcus sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, alphaCys112-SO2H and alphaCys114-SOH. We replaced alphaGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic center, with glutamic acid or asparagine. The kcat of alphaQ90E and alphaQ90N mutants decreased to 24% and 5% that of wild type respectively, but the effect of mutations on Km was not very significant. In both mutants, the alphaCys114-SOH modification appeared to be responsible for the catalysis as in native NHase. We crystallized the nitrosylated alphaQ90N mutant and determined its structure at a resolution of 1.43 A. The structure was basically identical to that of native nitrosylated NHase except for the mutated site and its vicinity. The structural difference between native and alphaQ90N mutant NHases suggested the importance of the hydrogen bond networks between alphaGln90 and the iron center for the catalytic activity.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
2ZCF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZCF OCA].
+
</div>
 +
<div class="pdbe-citations 2zcf" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
Mutational study on alphaGln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771., Takarada H, Kawano Y, Hashimoto K, Nakayama H, Ueda S, Yohda M, Kamiya N, Dohmae N, Maeda M, Odaka M, Biosci Biotechnol Biochem. 2006 Apr;70(4):881-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16636455 16636455]
+
*[[Nitrile hydratase|Nitrile hydratase]]
-
[[Category: Nitrile hydratase]]
+
== References ==
-
[[Category: Protein complex]]
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Rhodococcus erythropolis]]
[[Category: Rhodococcus erythropolis]]
-
[[Category: Dohmae, N.]]
+
[[Category: Dohmae N]]
-
[[Category: Hashimoto, K.]]
+
[[Category: Hashimoto K]]
-
[[Category: Kamiya, N.]]
+
[[Category: Kamiya N]]
-
[[Category: Kawano, Y.]]
+
[[Category: Kawano Y]]
-
[[Category: Maeda, M.]]
+
[[Category: Maeda M]]
-
[[Category: Nakayama, H.]]
+
[[Category: Nakayama H]]
-
[[Category: Odaka, M.]]
+
[[Category: Odaka M]]
-
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+
[[Category: Takarada H]]
-
[[Category: Takarada, H.]]
+
[[Category: Ueda S]]
-
[[Category: Ueda, S.]]
+
[[Category: Yohda M]]
-
[[Category: Yohda, M.]]
+
-
[[Category: Cysteine-sulfenic acid]]
+
-
[[Category: Cysteine-sulfinic acid]]
+
-
[[Category: Hydration]]
+
-
[[Category: Iron]]
+
-
[[Category: Lyase]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: National project on protein structural and functional analyse]]
+
-
[[Category: Nitrile]]
+
-
[[Category: Nppsfa]]
+
-
[[Category: Oxidation]]
+
-
[[Category: Photo-activation]]
+
-
[[Category: Photo-reactive]]
+
-
[[Category: Riken structural genomics/proteomics initiative]]
+
-
[[Category: Rsgi]]
+
-
[[Category: Structural genomic]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:08:29 2008''
+

Current revision

Mutational study on Alpha-Gln90 of Fe-type nitrile hydratase from Rhodococcus sp. N771

PDB ID 2zcf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools