2bp0: Difference between revisions

Revision as of 06:42, 16 May 2018

M144L mutant of nitrite reductase from Alcaligenes xylosoxidans

Structural highlights

2bp0 is a 2 chain structure with sequence from "achromobacter_xylosoxidans"_yabuuchi_and_ohyama_1971 "achromobacter xylosoxidans" yabuuchi and ohyama 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	CU, SO4, ZN
Related:	1bq5, 1gs6, 1gs7, 1gs8, 1hau, 1haw, 1ndt, 1oe1, 1oe2, 1oe3, 1wa0, 1wa1, 1wa2, 1wae, 2bo0, 2bp8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

We present high-resolution crystal structures and functional analysis of T1Cu centre mutants of nitrite reductase that perturb the redox potential and the Cys130-His129 "hard-wired" bridge through which electron transfer to the catalytic T2Cu centre occurs. These data provide insight into how activity can be altered through mutational manipulation of the electron delivery centre (T1Cu). The alteration of Cys to Ala results in loss of T1Cu and enzyme inactivation with azurin as electron donor despite the mutant enzyme retaining full nitrite-binding capacity. These data establish unequivocally that no direct transfer of electrons occurs from azurin to the catalytic type 2 Cu centre. The mutation of the axial ligand Met144 to Leu increases both the redox potential and catalytic activity, establishing that the rate-determining step of catalysis is the intermolecular electron transfer from azurin to nitrite reductase.

High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase.,Hough MA, Ellis MJ, Antonyuk S, Strange RW, Sawers G, Eady RR, Samar Hasnain S J Mol Biol. 2005 Jul 8;350(2):300-9. PMID:15927201^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hough MA, Ellis MJ, Antonyuk S, Strange RW, Sawers G, Eady RR, Samar Hasnain S. High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. J Mol Biol. 2005 Jul 8;350(2):300-9. PMID:15927201 doi:10.1016/j.jmb.2005.04.006

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Hough MA, Ellis MJ, Antonyuk S, Strange RW, Sawers G, Eady RR, Samar Hasnain S. High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. J Mol Biol. 2005 Jul 8;350(2):300-9. PMID:15927201 doi:10.1016/j.jmb.2005.04.006

[1]

@@ Line 1: / Line 1: @@
-==M144L MUTANT OF NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS==
+==M144L mutant of nitrite reductase from Alcaligenes xylosoxidans==
 <StructureSection load='2bp0' size='340' side='right' caption='[[2bp0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bq5|1bq5]], [[1gs6|1gs6]], [[1gs7|1gs7]], [[1gs8|1gs8]], [[1hau|1hau]], [[1haw|1haw]], [[1ndt|1ndt]], [[1oe1|1oe1]], [[1oe2|1oe2]], [[1oe3|1oe3]], [[1wa0|1wa0]], [[1wa1|1wa1]], [[1wa2|1wa2]], [[1wae|1wae]], [[2bo0|2bo0]], [[2bp8|2bp8]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bp0 OCA], [http://pdbe.org/2bp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bp0 RCSB], [http://www.ebi.ac.uk/pdbsum/2bp0 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bp0 OCA], [http://pdbe.org/2bp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bp0 RCSB], [http://www.ebi.ac.uk/pdbsum/2bp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bp0 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/2bp0_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/2bp0_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 ==See Also==
-*[[Nitric reductase|Nitric reductase]]
+*[[Nitrite reductase|Nitrite reductase]]
 == References ==
 <references/>

2bp0: Difference between revisions

Revision as of 06:42, 16 May 2018

M144L mutant of nitrite reductase from Alcaligenes xylosoxidans

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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