1et5: Difference between revisions

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New page: left|200px<br /><applet load="1et5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1et5, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1et5.jpg|left|200px]]<br /><applet load="1et5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1et5, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6'''<br />


==Overview==
==CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6==
Two active site residues, Asp-98 and His-255, of copper-containing nitrite, reductase (NIR) from Alcaligenes faecalis have been mutated to probe the, catalytic mechanism. Three mutations at these two sites (D98N, H255D, and, H255N) result in large reductions in activity relative to native NIR, suggesting that both residues are involved intimately in the reaction, mechanism. Crystal structures of these mutants have been determined using, data collected to better than 1. 9-A resolution. In the native structure, His-255 Nepsilon2 forms a hydrogen bond through a bridging water molecule, to the side chain of Asp-98, which also forms a hydrogen bond to a water, or nitrite oxygen ligated to the active site copper. In the D98N mutant, reorientation of the Asn-98 side chain results in the loss of the hydrogen, bond to the copper ligand water, consistent with a negatively charged, Asp-98 directing the binding and protonation of nitrite in the native, enzyme. An additional solvent molecule is situated between residues 255, and the bridging water in the H255N and H255D mutants and likely inhibits, nitrite binding. The interaction of His-255 with the bridging water, appears to be necessary for catalysis and may donate a proton to reaction, intermediates in addition to Asp-98.
<StructureSection load='1et5' size='340' side='right'caption='[[1et5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1et5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ET5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ET5 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1et5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1et5 OCA], [https://pdbe.org/1et5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1et5 RCSB], [https://www.ebi.ac.uk/pdbsum/1et5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1et5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NIR_ALCFA NIR_ALCFA]
== 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/et/1et5_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=1et5 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1ET5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with CU and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ET5 OCA].
*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase., Boulanger MJ, Kukimoto M, Nishiyama M, Horinouchi S, Murphy ME, J Biol Chem. 2000 Aug 4;275(31):23957-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10811642 10811642]
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
[[Category: Nitrite reductase (NO-forming)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Boulanger MJ]]
[[Category: Boulanger, M.J.]]
[[Category: Horinouchi S]]
[[Category: Horinouchi, S.]]
[[Category: Kukimoto M]]
[[Category: Kukimoto, M.]]
[[Category: Murphy MEP]]
[[Category: Murphy, M.E.P.]]
[[Category: Nishiyama M]]
[[Category: Nishiyama, M.]]
[[Category: CU]]
[[Category: ZN]]
[[Category: greek key beta barrel domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:17:40 2007''

Latest revision as of 10:06, 7 February 2024

CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6CRYSTAL STRUCTURE OF NITRITE REDUCTASE ASP98ASN MUTANT FROM ALCALIGENES FAECALIS S-6

Structural highlights

1et5 is a 1 chain structure with sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NIR_ALCFA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1et5, resolution 1.90Å

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