1cuo

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J

Structural highlights

1cuo is a 1 chain structure with sequence from Methylomonas sp. J. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AZUR2_METJ This methylothroph organism uses azurin in the oxidation of methylamine. Iso-2 is probably the acceptor of electrons from methylamine dehydrogenase.

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

The obligate methylotroph Methylomonas sp. strain J produces two azurins (Az-iso1 and Az-iso2) as candidates for electron acceptor from methylamine dehydrogenase (MADH) in the electron-transfer process involving the oxidation of methylamine to formaldehyde and ammonia. The X-ray crystallographic study indicated that Az-iso2 gives two types of crystals (form I and form II) with polyethylene glycol (PEG4000) and ammonium sulfate as the precipitants, respectively. Comparison between the two Az-iso2 structures in forms I and II reveals the remarkable structural changes at the top surface of the molecule around the copper atom. Az-iso2 possesses Gly43 instead of Val43 or Ala43, which is unique among all other azurins around the copper ligand His46, inducing the remarkable structural change in the loop region from Gly37 to Gly43. When the structure of Az-iso2 is superimposed on that of amicyanin in the ternary complex composed of MADH, amicyanin, and cytochrome c(551), the loop of Az-iso2 deeply overlaps with the light subunit of MADH. However, the Az-iso2 molecule is probably able to avoid any steric hindrance with the cognate MADH to form the complex for intermolecular electron-transfer reaction, since the loop containing Gly43 is flexible. We discuss why the electron-transfer activity of Az-iso2 is fivefold higher than that of Az-iso1.

The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J.,Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:14516747^[1]

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

References

↑ Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y. The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J. J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:14516747

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cuo"

@@ Line 3: / Line 3: @@
 <StructureSection load='1cuo' size='340' side='right'caption='[[1cuo]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cuo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylomonas_sp._j Methylomonas sp. j]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CUO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cuo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylomonas_sp._J Methylomonas sp. J]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CUO 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></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=1cuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cuo OCA], [http://pdbe.org/1cuo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cuo RCSB], [http://www.ebi.ac.uk/pdbsum/1cuo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cuo ProSAT]</span></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cuo OCA], [https://pdbe.org/1cuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cuo RCSB], [https://www.ebi.ac.uk/pdbsum/1cuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cuo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AZUR2_METJ AZUR2_METJ]] This methylothroph organism uses azurin in the oxidation of methylamine. Iso-2 is probably the acceptor of electrons from methylamine dehydrogenase.
+[https://www.uniprot.org/uniprot/AZUR2_METJ AZUR2_METJ] This methylothroph organism uses azurin in the oxidation of methylamine. Iso-2 is probably the acceptor of electrons from methylamine dehydrogenase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/1cuo_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 36: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Methylomonas sp. j]]
+[[Category: Methylomonas sp. J]]
-[[Category: Inoue, T]]
+[[Category: Inoue T]]
-[[Category: Kai, Y]]
+[[Category: Kai Y]]
-[[Category: Kataoka, K]]
+[[Category: Kataoka K]]
-[[Category: Nishio, N]]
+[[Category: Nishio N]]
-[[Category: Suzuki, S]]
+[[Category: Suzuki S]]
-[[Category: Beta barrel]]
-[[Category: Electron transport]]
-[[Category: Periplasmic]]

1cuo

From Proteopedia

Current revision

CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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