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2ov3

From Proteopedia

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Crystal structure of 138-173 ZnuA deletion mutant plus zinc bound

Structural highlights

2ov3 is a 1 chain structure with sequence from Synechocystis sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

P73085_SYNY3

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

A number of bacterial metal transporters belong to the ABC transporter family. To better understand the structural determinants of metal selectivity of one such transporter, we previously determined the structure of the periplasmic domain of a zinc transporter, ZnuA, from Synechocystis 6803 and found that ZnuA binds zinc via three histidines. Unique to these ABC zinc transporters, ZnuA has a highly charged and mobile loop that protrudes from the protein in the vicinity of the metal binding site that we had suggested might facilitate zinc acquisition. To further examine the function of this loop, the structure and zinc binding properties of two ZnuA variants were determined. When the loop is entirely deleted, zinc still binds to the three histidines. However, unlike what was suggested from the structure of a similar solute binding protein, TroA, release of zinc occurs concomitantly with large conformational changes in two of the three chelating histidines. These structural results combined with isothermal titration calorimetry data demonstrate that there are at least two classes of zinc binding sites: the high-affinity site in the cleft between the two domains and at least one additional site on the flexible loop. This loop has approximately 100-fold weaker affinity for zinc than the high-affinity zinc binding site, and its deletion does not affect the high-affinity site. From these results, we suggest that this region might be a sensor for high periplasmic levels of zinc.

Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA.,Wei B, Randich AM, Bhattacharyya-Pakrasi M, Pakrasi HB, Smith TJ Biochemistry. 2007 Jul 31;46(30):8734-43. Epub 2007 Jul 6. PMID:17616151^[1]

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

References

↑ Wei B, Randich AM, Bhattacharyya-Pakrasi M, Pakrasi HB, Smith TJ. Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA. Biochemistry. 2007 Jul 31;46(30):8734-43. Epub 2007 Jul 6. PMID:17616151 doi:10.1021/bi700763w

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/2ov3"

Categories: Large Structures | Synechocystis sp | Smith TJ | Wei B

@@ Line 1: / Line 1: @@
 ==Crystal structure of 138-173 ZnuA deletion mutant plus zinc bound==
-<StructureSection load='2ov3' size='340' side='right' caption='[[2ov3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='2ov3' size='340' side='right'caption='[[2ov3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ov3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cyanobacterium_synechocystis Cyanobacterium synechocystis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OV3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ov3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OV3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ov1|2ov1]], [[1pq4|1pq4]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zntC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Cyanobacterium synechocystis])</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=2ov3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ov3 OCA], [https://pdbe.org/2ov3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ov3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ov3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ov3 ProSAT]</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=2ov3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ov3 OCA], [http://pdbe.org/2ov3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ov3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ov3 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/P73085_SYNY3 P73085_SYNY3]
 == 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/ov/2ov3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ov/2ov3_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 31: @@
 ==See Also==
-*[[ABC transporter|ABC transporter]]
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cyanobacterium synechocystis]]
+[[Category: Large Structures]]
-[[Category: Smith, T J]]
+[[Category: Synechocystis sp]]
-[[Category: Wei, B]]
+[[Category: Smith TJ]]
-[[Category: Abc transporter]]
+[[Category: Wei B]]
-[[Category: Solute binding domain]]
-[[Category: Transport protein]]
-[[Category: Zinc transport]]

2ov3

From Proteopedia

Current revision

Crystal structure of 138-173 ZnuA deletion mutant plus zinc bound

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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