2i6w
From Proteopedia
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| - | [[Image:2i6w.jpg|left|200px]] | + | [[Image:2i6w.jpg|left|200px]] |
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| - | '''Crystal structure of the multidrug efflux transporter AcrB''' | + | {{Structure |
| + | |PDB= 2i6w |SIZE=350|CAPTION= <scene name='initialview01'>2i6w</scene>, resolution 3.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the multidrug efflux transporter AcrB''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2I6W is a [ | + | 2I6W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I6W OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids., Das D, Xu QS, Lee JY, Ankoudinova I, Huang C, Lou Y, DeGiovanni A, Kim R, Kim SH, J Struct Biol. 2007 Jun;158(3):494-502. Epub 2006 Dec 24. PMID:[http:// | + | Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids., Das D, Xu QS, Lee JY, Ankoudinova I, Huang C, Lou Y, DeGiovanni A, Kim R, Kim SH, J Struct Biol. 2007 Jun;158(3):494-502. Epub 2006 Dec 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17275331 17275331] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: multidrug efflux transporter]] | [[Category: multidrug efflux transporter]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:26:12 2008'' |
Revision as of 15:26, 20 March 2008
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Crystal structure of the multidrug efflux transporter AcrB
Overview
Crystal structures of the bacterial multidrug transporter AcrB in R32 and C2 space groups showing both symmetric and asymmetric trimeric assemblies, respectively, supplemented with biochemical investigations, have provided most of the structural basis for a molecular level understanding of the protein structure and mechanisms for substrate uptake and translocation carried out by this 114-kDa inner membrane protein. They suggest that AcrB captures ligands primarily from the periplasm. Substrates can also enter the inner cavity of the transporter from the cytoplasm, but the exact mechanism of this remains undefined. Analysis of the amino acid sequences of AcrB and its homologs revealed the presence of conserved residues at the N-terminus including two phenylalanines which may be exposed to the cytoplasm. Any potential role that these conserved residues may play in function has not been addressed by existing biochemical or structural studies. Since phenylalanine residues elsewhere in the protein have been implicated in ligand binding, we explored the structure of this N-terminal region to investigate structural determinants near the cytoplasmic opening that may mediate drug uptake. Our structure of AcrB in R32 space group reveals an N-terminus loop, reducing the diameter of the central opening to approximately 15 A as opposed to the previously reported value of approximately 30 A for crystal structures in this space group with disordered N-terminus. Recent structures of the AcrB in C2 space group have revealed a helical conformation of this N-terminus but have not discussed its possible implications. We present the crystal structure of AcrB that reveals the structure of the N-terminus containing the conserved residues. We hope that the structural information provides a structural basis for others to design further biochemical investigation of the role of this portion of AcrB in mediating cytoplasmic ligand discrimination and uptake.
About this Structure
2I6W is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the multidrug efflux transporter AcrB at 3.1A resolution reveals the N-terminal region with conserved amino acids., Das D, Xu QS, Lee JY, Ankoudinova I, Huang C, Lou Y, DeGiovanni A, Kim R, Kim SH, J Struct Biol. 2007 Jun;158(3):494-502. Epub 2006 Dec 24. PMID:17275331
Page seeded by OCA on Thu Mar 20 17:26:12 2008
