2c7g

From Proteopedia

(Difference between revisions)

Revision as of 08:15, 23 May 2018

FprA from Mycobacterium tuberculosis: His57Gln mutant

Structural highlights

2c7g is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1lqt, 1lqu
Activity:	Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FPRA_MYCTU] May serve as electron transfer protein and supply electrons to P450 systems.

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

Mycobacterium tuberculosis FprA is a NADPH-ferredoxin reductase, functionally and structurally similar to the mammalian adrenodoxin reductase. It is presumably involved in supplying electrons to one or more of the pathogen's cytochrome P450s through reduced ferredoxins. It has been proposed on the basis of crystallographic data (Bossi, R. T., et al. (2002) Biochemistry 41, 8807-8818) that the highly conserved His57 and Glu214 whose side chains are H-bonded are involved in catalysis. Both residues were individually changed to nonionizable amino acyl residues through site-directed mutagenesis. Steady-state kinetics showed that the role of Glu214 in catalysis is negligible. On the contrary, the substitutions of His57 markedly impaired the catalytic efficiency of FprA for ferredoxin in the physiological reaction. Furthemore, they decreased the k(cat)/K(m) value for NADPH in the ferricyanide reduction. Rapid-reaction (stopped-flow) kinetic analysis of the isolated reductive half-reaction of wild-type and His57Gln forms of FprA with NADPH and NADH allowed a detailed description of the mechanism of enzyme-bound FAD reduction, with the identification of the intermediates involved. The His57Gln mutation caused a 6-fold decrease in the rate of hydride transfer from either NADPH or NADH to the enzyme-bound FAD cofactor. The 3D structure of FprA-H57Q, obtained at 1.8 A resolution, explains the inefficient hydride transfer of the mutant in terms of a suboptimal geometry of the nicotinamide-isoalloxazine interaction in the active site. These data demonstrate the role of His57 in the correct binding of NADPH to FprA for the subsequent steps of the catalytic cycle to proceed at a high rate.

Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA.,Pennati A, Razeto A, de Rosa M, Pandini V, Vanoni MA, Mattevi A, Coda A, Aliverti A, Zanetti G Biochemistry. 2006 Jul 25;45(29):8712-20. PMID:16846214^[1]

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

References

↑ Pennati A, Razeto A, de Rosa M, Pandini V, Vanoni MA, Mattevi A, Coda A, Aliverti A, Zanetti G. Role of the His57-Glu214 ionic couple located in the active site of Mycobacterium tuberculosis FprA. Biochemistry. 2006 Jul 25;45(29):8712-20. PMID:16846214 doi:10.1021/bi060369m

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c7g"

@@ Line 1: / Line 1: @@
-==FPRA FROM MYCOBACTERIUM TUBERCULOSIS: HIS57GLN MUTANT==
+==FprA from Mycobacterium tuberculosis: His57Gln mutant==
 <StructureSection load='2c7g' size='340' side='right' caption='[[2c7g]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lqt|1lqt]], [[1lqu|1lqu]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </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=2c7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7g OCA], [http://pdbe.org/2c7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c7g RCSB], [http://www.ebi.ac.uk/pdbsum/2c7g 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=2c7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7g OCA], [http://pdbe.org/2c7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c7g RCSB], [http://www.ebi.ac.uk/pdbsum/2c7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7g ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/2c7g_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/2c7g_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2c7g

From Proteopedia

Revision as of 08:15, 23 May 2018

FprA from Mycobacterium tuberculosis: His57Gln mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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