2ov1
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2ov1.jpg|left|200px]] | [[Image:2ov1.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2ov1", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2ov1| PDB=2ov1 | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Crystal structure of apo form of ZnuA with flexible loop deletion''' | '''Crystal structure of apo form of ZnuA with flexible loop deletion''' | ||
| Line 27: | Line 24: | ||
[[Category: Smith, T J.]] | [[Category: Smith, T J.]] | ||
[[Category: Wei, B.]] | [[Category: Wei, B.]] | ||
| - | [[Category: | + | [[Category: Abc transporter]] |
| - | [[Category: | + | [[Category: Solute binding domain]] |
| - | [[Category: | + | [[Category: Transport protein]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 08:43, 4 May 2008
Crystal structure of apo form of ZnuA with flexible loop deletion
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
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 May 4 11:43:04 2008
