2ov3
From Proteopedia
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|PDB= 2ov3 |SIZE=350|CAPTION= <scene name='initialview01'>2ov3</scene>, resolution 2.400Å | |PDB= 2ov3 |SIZE=350|CAPTION= <scene name='initialview01'>2ov3</scene>, resolution 2.400Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= zntC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]) | |GENE= zntC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ov1|2OV1]], [[1pq4|1PQ4]] | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/2ov3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ov3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Smith, T J.]] | [[Category: Smith, T J.]] | ||
[[Category: Wei, B.]] | [[Category: Wei, B.]] | ||
| - | [[Category: ZN]] | ||
[[Category: abc transporter]] | [[Category: abc transporter]] | ||
[[Category: solute binding domain]] | [[Category: solute binding domain]] | ||
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[[Category: zinc transport]] | [[Category: zinc transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:36 2008'' |
Revision as of 01:23, 31 March 2008
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| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | zntC (Synechocystis sp.) | ||||||
| Related: | 2OV1, 1PQ4
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of 138-173 ZnuA deletion mutant plus zinc bound
Overview
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.
About this Structure
2OV3 is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
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
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