1e30

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:30, 13 August 2025) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1e30.gif|left|200px]]
 
-
<!--
+
==Crystal structure of the Met148Gln mutant of rusticyanin at 1.5 Angstrom resolution==
-
The line below this paragraph, containing "STRUCTURE_1e30", creates the "Structure Box" on the page.
+
<StructureSection load='1e30' size='340' side='right'caption='[[1e30]], [[Resolution|resolution]] 1.50&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'>[[1e30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E30 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]] 1.5&#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></td></tr>
-
{{STRUCTURE_1e30| PDB=1e30 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e30 OCA], [https://pdbe.org/1e30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e30 RCSB], [https://www.ebi.ac.uk/pdbsum/1e30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e30 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RUS2_ACIFI RUS2_ACIFI] Electron carrier from cytochrome c552 to the A-type oxidase.
 +
== 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/e3/1e30_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=1e30 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Type 1 Cu centers in cupredoxins, nitrite reductases, and multi-copper oxidases utilize the same trigonal core ligation to His-Cys-His, with a weak axial ligand generally provided by a Met sulfur. In azurin, an additional axial ligand, a carbonyl oxygen from a Gly, is present. The importance of these axial ligands and in particular the Met has been debated extensively in terms of their role in fine-tuning the redox potential, spectroscopic properties, and rack-induced or entatic state properties of the copper sites. Extensive site-directed mutagenesis of the Met ligand has been carried out in azurin, but the presence of an additional carbonyl oxygen axial ligand has made it difficult to interpret the effects of these substitutions. Here, the axial methionine ligand (Met148) in rusticyanin is replaced with Leu, Gln, Lys, and Glu to examine the effect on the redox potential, acid stability, and copper site geometry. The midpoint redox potential varies from 363 (Met148Lys) to 798 mV (Met148Leu). The acid stability of the oxidized proteins is reduced except for the Met148Gln mutant. The Gln mutant remains blue at all pH values between 2.8 and 8, and has a redox potential of 563 mV at pH 3.2. The optical and rhombic EPR properties of this mutant closely resemble those of stellacyanin, which has the lowest redox potential among single-type 1 copper proteins (185 mV). The Met148Lys mutant exhibits type 2 Cu EPR and optical spectra in this pH range. The Met148Glu mutant exhibits a type 2 Cu EPR spectrum above pH 3 and a mixture of type 1 and type 2 Cu spectra at lower pH. The Met148Leu mutant exhibits the highest redox potential ( approximately 800 mV at pH 3.2) which is similar to the values in fungal laccase and in the type 1 Cu site of ceruloplasmin where this axial ligand is also a Leu.
-
'''CRYSTAL STRUCTURE OF THE MET148GLN MUTANT OF RUSTICYANIN AT 1.5 ANGSTROM RESOLUTION'''
+
Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin.,Hall JF, Kanbi LD, Strange RW, Hasnain SS Biochemistry. 1999 Sep 28;38(39):12675-80. PMID:10504237<ref>PMID:10504237</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==Overview==
+
</div>
-
The small blue copper protein rusticyanin from Thiobacillus ferrooxidans contains a type 1 Cu centre with a single axial ligand, Met148, which together with the His-Cys-His trigonal planar ligands produces a distorted trigonal pyramidal coordination geometry to copper. Type 1 Cu sites are found in cupredoxins and several multicopper proteins, including oxidases and nitrite reductases. The role of the axial ligand has been extensively debated in terms of its function in the fine tuning of the redox potential and spectroscopic properties of type 1 Cu sites. Numerous mutations of the Met ligand in azurins have been studied, but interpretation of the results has been complicated by the presence of the additional carbonyl oxygen ligand from Gly45, a neighbouring residue to the coordinating His46. The importance of the axial ligand has been further emphasized by the finding that the type 1 centre in Rhus vernicifera stellacyanin, with the lowest redox potential in a type 1 Cu site of 184 mV, has Gln as the axial ligand, whilst fungal laccase and ceruloplasmin, which have redox potentials of 550-800 mV, have a Leu in this position. Here, the crystal structure of the M148Q mutant of rusticyanin at 1.5 A resolution is presented. This is a significantly higher resolution than that of the structures of native rusticyanin. In addition, the M148Q structure is that of the oxidized protein while the native structures to date are of the reduced protein. The mutant protein crystallizes with two molecules per asymmetric unit, in contrast to the one present in the native crystal form. This mutant's redox potential (550 mV at pH 3.2) is lowered compared with that of the native protein ( approximately 670 mV at pH 3.2) by about 120 mV. The type 1 Cu site of M148Q closely mimics the structural characteristics of the equivalent site in non-glycosylated cucumber stellacyanin (redox potential approximately 260 mV) and, owing to the absence in rusticyanin of the fifth, carbonyl ligand present in azurin, may provide a better model for the R. vernicifera stellacyanin (redox potential approximately 184 mV) type 1 Cu site, which also lacks the fifth ligand. Furthermore, the presence of two molecules in the asymmetric unit cell indicates a potential binding region of the redox partners.
+
<div class="pdbe-citations 1e30" style="background-color:#fffaf0;"></div>
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1E30 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E30 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Structure of the M148Q mutant of rusticyanin at 1.5 A: a model for the copper site of stellacyanin., Hough MA, Hall JF, Kanbi LD, Hasnain SS, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):355-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11223511 11223511]
+
[[Category: Acidithiobacillus ferrooxidans]]
[[Category: Acidithiobacillus ferrooxidans]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Hasnain, S S.]]
+
[[Category: Hasnain SS]]
-
[[Category: Hough, M A.]]
+
[[Category: Hough MA]]
-
[[Category: Strange, R W.]]
+
[[Category: Strange RW]]
-
[[Category: Axial ligand]]
+
-
[[Category: Cupredoxin]]
+
-
[[Category: Mutant]]
+
-
[[Category: Rusticyanin]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:35:46 2008''
+

Current revision

Crystal structure of the Met148Gln mutant of rusticyanin at 1.5 Angstrom resolution

PDB ID 1e30

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e30"
Personal tools