1u7c: Difference between revisions
New page: left|200px<br /><applet load="1u7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7c, resolution 1.85Å" /> '''Crystal Structure of... |
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[[Image:1u7c.jpg|left|200px]]<br /><applet load="1u7c" size=" | [[Image:1u7c.jpg|left|200px]]<br /><applet load="1u7c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1u7c, resolution 1.85Å" /> | caption="1u7c, resolution 1.85Å" /> | ||
'''Crystal Structure of AmtB from E.Coli with Methyl Ammonium.'''<br /> | '''Crystal Structure of AmtB from E.Coli with Methyl Ammonium.'''<br /> | ||
==Overview== | ==Overview== | ||
The first structure of an ammonia channel from the Amt/MEP/Rh protein | The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3. | ||
==About this Structure== | ==About this Structure== | ||
1U7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1U7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NME:'>NME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7C OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: III, J | [[Category: III, J O.Connell.]] | ||
[[Category: Khademi, S.]] | [[Category: Khademi, S.]] | ||
[[Category: Miercke, L | [[Category: Miercke, L J.W.]] | ||
[[Category: Remis, J.]] | [[Category: Remis, J.]] | ||
[[Category: Robles-Colmenares, Y.]] | [[Category: Robles-Colmenares, Y.]] | ||
[[Category: Stroud, R | [[Category: Stroud, R M.]] | ||
[[Category: NME]] | [[Category: NME]] | ||
[[Category: ammonia channel]] | [[Category: ammonia channel]] | ||
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[[Category: transmembrane helices]] | [[Category: transmembrane helices]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:19 2008'' |
Revision as of 16:21, 21 February 2008
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Crystal Structure of AmtB from E.Coli with Methyl Ammonium.
OverviewOverview
The first structure of an ammonia channel from the Amt/MEP/Rh protein superfamily, determined to 1.35 angstrom resolution, shows it to be a channel that spans the membrane 11 times. Two structurally similar halves span the membrane with opposite polarity. Structures with and without ammonia or methyl ammonia show a vestibule that recruits NH4+/NH3, a binding site for NH4+, and a 20 angstrom-long hydrophobic channel that lowers the NH4+ pKa to below 6 and conducts NH3. Favorable interactions for NH3 are seen within the channel and use conserved histidines. Reconstitution of AmtB into vesicles shows that AmtB conducts uncharged NH3.
About this StructureAbout this Structure
1U7C is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 A., Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, Stroud RM, Science. 2004 Sep 10;305(5690):1587-94. PMID:15361618
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