From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2bbh.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2bbh.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2bbh| PDB=2bbh | SCENE= }} | | {{STRUCTURE_2bbh| PDB=2bbh | SCENE= }} |
| | | | |
| - | '''X-ray structure of T.maritima CorA soluble domain'''
| + | ===X-ray structure of T.maritima CorA soluble domain=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The magnesium ion, Mg2+, is essential for myriad biochemical processes and remains the only major biological ion whose transport mechanisms remain unknown. The CorA family of magnesium transporters is the primary Mg2+ uptake system of most prokaryotes and a functional homologue of the eukaryotic mitochondrial magnesium transporter. Here we determine crystal structures of the full-length Thermotoga maritima CorA in an apparent closed state and its isolated cytoplasmic domain at 3.9 A and 1.85 A resolution, respectively. The transporter is a funnel-shaped homopentamer with two transmembrane helices per monomer. The channel is formed by an inner group of five helices and putatively gated by bulky hydrophobic residues. The large cytoplasmic domain forms a funnel whose wide mouth points into the cell and whose walls are formed by five long helices that are extensions of the transmembrane helices. The cytoplasmic neck of the pore is surrounded, on the outside of the funnel, by a ring of highly conserved positively charged residues. Two negatively charged helices in the cytoplasmic domain extend back towards the membrane on the outside of the funnel and abut the ring of positive charge. An apparent Mg2+ ion was bound between monomers at a conserved site in the cytoplasmic domain, suggesting a mechanism to link gating of the pore to the intracellular concentration of Mg2+. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16598263}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16598263 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16598263}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 36: |
Line 40: |
| | [[Category: Structural genomics consortium]] | | [[Category: Structural genomics consortium]] |
| | [[Category: Transporter]] | | [[Category: Transporter]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:04:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:13:36 2008'' |
Revision as of 14:13, 28 July 2008
Template:STRUCTURE 2bbh
X-ray structure of T.maritima CorA soluble domain
Template:ABSTRACT PUBMED 16598263
About this Structure
2BBH is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of the CorA Mg2+ transporter., Lunin VV, Dobrovetsky E, Khutoreskaya G, Zhang R, Joachimiak A, Doyle DA, Bochkarev A, Maguire ME, Edwards AM, Koth CM, Nature. 2006 Apr 6;440(7085):833-7. PMID:16598263
Page seeded by OCA on Mon Jul 28 17:13:36 2008
