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| - | [[Image:2ov1.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2ov1| PDB=2ov1 | SCENE= }} | | {{STRUCTURE_2ov1| PDB=2ov1 | SCENE= }} |
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| - | '''Crystal structure of apo form of ZnuA with flexible loop deletion'''
| + | ===Crystal structure of apo form of ZnuA with flexible loop deletion=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17616151}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17616151 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17616151}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Transport protein]] | | [[Category: Transport protein]] |
| | [[Category: Zinc transporter]] | | [[Category: Zinc transporter]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:43:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:26:53 2008'' |
Revision as of 15:26, 27 July 2008
Template:STRUCTURE 2ov1
Crystal structure of apo form of ZnuA with flexible loop deletion
Template:ABSTRACT PUBMED 17616151
About this Structure
2OV1 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
Page seeded by OCA on Sun Jul 27 18:26:53 2008
