2bbh: Difference between revisions
New page: left|200px<br /><applet load="2bbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bbh, resolution 1.85Å" /> '''X-ray structure of T... |
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[[Image:2bbh.gif|left|200px]]<br /><applet load="2bbh" size=" | [[Image:2bbh.gif|left|200px]]<br /><applet load="2bbh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bbh, resolution 1.85Å" /> | caption="2bbh, resolution 1.85Å" /> | ||
'''X-ray structure of T.maritima CorA soluble domain'''<br /> | '''X-ray structure of T.maritima CorA soluble domain'''<br /> | ||
==Overview== | ==Overview== | ||
The magnesium ion, Mg2+, is essential for myriad biochemical processes and | 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+. | ||
==About this Structure== | ==About this Structure== | ||
2BBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with DMU, NA and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2BBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=DMU:'>DMU</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bochkarev, A.]] | [[Category: Bochkarev, A.]] | ||
[[Category: Dobrovetsky, E.]] | [[Category: Dobrovetsky, E.]] | ||
[[Category: Edwards, A | [[Category: Edwards, A M.]] | ||
[[Category: Khutoreskaya, G.]] | [[Category: Khutoreskaya, G.]] | ||
[[Category: Koth, C | [[Category: Koth, C M.]] | ||
[[Category: Lunin, V | [[Category: Lunin, V V.]] | ||
[[Category: Maguire, M | [[Category: Maguire, M E.]] | ||
[[Category: SGC, Structural | [[Category: SGC, Structural Genomics Consortium.]] | ||
[[Category: DMU]] | [[Category: DMU]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: transporter]] | [[Category: transporter]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:01 2008'' | ||
Revision as of 17:36, 21 February 2008
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X-ray structure of T.maritima CorA soluble domain
OverviewOverview
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+.
About this StructureAbout this Structure
2BBH is a Single protein structure of sequence from Thermotoga maritima with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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