|
|
| Line 1: |
Line 1: |
| [[Image:2osv.gif|left|200px]] | | {{Seed}} |
| | [[Image:2osv.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2osv| PDB=2osv | SCENE= }} | | {{STRUCTURE_2osv| PDB=2osv | SCENE= }} |
|
| |
|
| '''Crystal Structure of ZnuA from E. coli'''
| | ===Crystal Structure of ZnuA from E. coli=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| Bacterial ATP-binding cassette transport systems for high-affinity uptake of zinc and manganese use a cluster 9 solute-binding protein. Structures of four cluster 9 transport proteins have been determined previously. However, the structural determinants for discrimination between zinc and manganese remain under discussion. To further investigate the variability of metal binding sites in bacterial transporters, we have determined the structure of the zinc-bound transport protein ZnuA from Escherichia coli to 1.75 A resolution. The overall structure of ZnuA is similar to other solute-binding transporters. A scaffolding alpha-helix forms the backbone for two structurally related globular domains. The metal-binding site is located at the domain interface. The bound zinc ion is coordinated by three histidine residues (His78, His161 and His225) and one glutamate residue (Glu77). The functional role of Glu77 for metal binding is unexpected, because this residue is not conserved in previously determined structures of zinc and manganese-specific transport proteins. The observed metal coordination by four protein residues differs significantly from the zinc-binding site in the ZnuA transporter from Synechocystis 6803, which binds zinc via three histidine residues. In addition, the E. coli ZnuA structure reveals the presence of a disulfide bond in the C-terminal globular domain that is not present in previously determined cluster 9 transport protein structures.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17399739}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17399739 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_17399739}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 25: |
Line 29: |
| [[Category: Li, H.]] | | [[Category: Li, H.]] |
| [[Category: Protein-zinc complex]] | | [[Category: Protein-zinc complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:35:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:10:56 2008'' |
