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4akp

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Revision as of 09:03, 6 March 2019

Mutations in the neighbourhood of CotA-laccase trinuclear site: E498T mutant

Structural highlights

4akp is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	1gsk, 1of0, 1uvw, 1w6l, 1w6w, 1w8e, 2bhf, 2x87, 2x88, 4a66, 4a67, 4a68, 4ako, 4akq
Activity:	Laccase, with EC number 1.10.3.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COTA_BACSU] Involved in brown pigmentation during sporogenesis.

Publication Abstract from PubMed

The multicopper oxidases couple the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen. This reduction takes place at the trinuclear copper centre of the enzyme and the dioxygen approaches this centre through an entrance channel. In this channel, an acidic residue plays a key role in steering the dioxygen to the trinuclear copper site, providing protons for the catalytic reaction and giving overall stability to this site. In this study, the role of the Glu(498) residue, located within the entrance channel to the trinuclear copper centre, has been investigated in the binding and reduction of dioxygen by the CotA-laccase from Bacillus subtilis. The absence of an acidic group at the 498 residue, as in the E498T and E498L mutants, results in a severe catalytic impairment, higher than 99%, for the phenolic and non-phenolic substrates tested. The replacement of this glutamate by aspartate leads to an activity that is around 10% relative to that of the wild-type. Furthermore, while this latter mutant shows a similar K(m) value for dioxygen, the E498T and E498L mutants show a decreased affinity, when compared to the wild-type. X-ray structural and spectroscopic analysis (UV-visible, electron paramagnetic resonance and resonance Raman) reveal perturbations of the structural properties of the catalytic centres in the Glu(498) mutants when compared to the wild-type protein. Overall, the results strongly suggest that Glu(498) plays a key role in the protonation events that occur at the trinuclear centre and in its stabilization, controlling therefore the binding of dioxygen and its further reduction.

The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis.,Chen Z, Durao P, Silva CS, Pereira MM, Todorovic S, Hildebrandt P, Bento I, Lindley PF, Martins LO Dalton Trans. 2010 Mar 21;39(11):2875-82. Epub 2010 Feb 5. PMID:20200715^[1]

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

References

↑ Chen Z, Durao P, Silva CS, Pereira MM, Todorovic S, Hildebrandt P, Bento I, Lindley PF, Martins LO. The role of Glu498 in the dioxygen reactivity of CotA-laccase from Bacillus subtilis. Dalton Trans. 2010 Mar 21;39(11):2875-82. Epub 2010 Feb 5. PMID:20200715 doi:10.1039/b922734b

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4akp"

@@ Line 1: / Line 1: @@
 ==Mutations in the neighbourhood of CotA-laccase trinuclear site: E498T mutant==
-<StructureSection load='4akp' size='340' side='right' caption='[[4akp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4akp' size='340' side='right'caption='[[4akp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4akp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AKP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4akp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AKP FirstGlance]. <br>
 </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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr>
@@ Line 28: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Vibrio subtilis ehrenberg 1835]]
 [[Category: Laccase]]
 [[Category: Bento, I]]

4akp

From Proteopedia

Revision as of 09:03, 6 March 2019

Mutations in the neighbourhood of CotA-laccase trinuclear site: E498T mutant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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