2bbj: Difference between revisions

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[[Image:2bbj.gif|left|200px]]<br /><applet load="2bbj" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2bbj.gif|left|200px]]<br /><applet load="2bbj" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2bbj, resolution 3.90Å" />

'''Crystal structure of the CorA Mg2+ transporter'''<br />

==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 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==

2BBJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2BBJ OCA].

2BBJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBJ OCA].

==Reference==

Line 15:

[[Category: Bochkarev, A.]]

[[Category: Dobrovetsky, E.]]

[[Category: Edwards, A.M.]]

[[Category: Edwards, A M.]]

[[Category: Joachimiak, A.]]

[[Category: Khutoreskaya, G.]]

[[Category: Koth, C.M.]]

[[Category: Koth, C M.]]

[[Category: Lunin, V.V.]]

[[Category: Lunin, V V.]]

[[Category: Maguire, M.E.]]

[[Category: Maguire, M E.]]

[[Category: SGC, Structural.Genomics.Consortium.]]

[[Category: SGC, Structural Genomics Consortium.]]

[[Category: Zhang, R.]]

[[Category: membrane]]

Line 31:

[[Category: transporter]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2bbj.gif|left|200px]]<br /><applet load="2bbj" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bbj.gif|left|200px]]<br /><applet load="2bbj" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bbj, resolution 3.90&Aring;" />
 '''Crystal structure of the CorA Mg2+ transporter'''<br />
 ==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 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==
-BBJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BBJ OCA].
+BBJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBJ OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Bochkarev, A.]]
 [[Category: Dobrovetsky, E.]]
-[[Category: Edwards, A.M.]]
+[[Category: Edwards, A M.]]
 [[Category: Joachimiak, A.]]
 [[Category: Khutoreskaya, G.]]
-[[Category: Koth, C.M.]]
+[[Category: Koth, C M.]]
-[[Category: Lunin, V.V.]]
+[[Category: Lunin, V V.]]
-[[Category: Maguire, M.E.]]
+[[Category: Maguire, M E.]]
-[[Category: SGC, Structural.Genomics.Consortium.]]
+[[Category: SGC, Structural Genomics Consortium.]]
 [[Category: Zhang, R.]]
 [[Category: membrane]]
@@ Line 31: / Line 31: @@
 [[Category: transporter]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:42:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:01 2008''