3wmg
From Proteopedia
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| - | ''' | + | ==Crystal structure of an inward-facing eukaryotic ABC multidrug transporter G277V/A278V/A279V mutant in complex with an cyclic peptide inhibitor, aCAP== |
| + | <StructureSection load='3wmg' size='340' side='right' caption='[[3wmg]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | [[3wmg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMG OCA]. <br> | ||
| + | <b>Related:</b> [[3wme|3wme]], [[3wmf|3wmf]]<br> | ||
| + | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
| + | == Publication Abstract from PubMed == | ||
| + | P-glycoprotein is an ATP-binding cassette multidrug transporter that actively transports chemically diverse substrates across the lipid bilayer. The precise molecular mechanism underlying transport is not fully understood. Here, we present crystal structures of a eukaryotic P-glycoprotein homolog, CmABCB1 from Cyanidioschyzon merolae, in two forms: unbound at 2.6-A resolution and bound to a unique allosteric inhibitor at 2.4-A resolution. The inhibitor clamps the transmembrane helices from the outside, fixing the CmABCB1 structure in an inward-open conformation similar to the unbound structure, confirming that an outward-opening motion is required for ATP hydrolysis cycle. These structures, along with site-directed mutagenesis and transporter activity measurements, reveal the detailed architecture of the transporter, including a gate that opens to extracellular side and two gates that open to intramembranous region and the cytosolic side. We propose that the motion of the nucleotide-binding domain drives those gating apparatuses via two short intracellular helices, IH1 and IH2, and two transmembrane helices, TM2 and TM5. | ||
| - | + | Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog.,Kodan A, Yamaguchi T, Nakatsu T, Sakiyama K, Hipolito CJ, Fujioka A, Hirokane R, Ikeguchi K, Watanabe B, Hiratake J, Kimura Y, Suga H, Ueda K, Kato H Proc Natl Acad Sci U S A. 2014 Mar 3. PMID:24591620<ref>PMID:24591620</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Fujioka, A.]] | ||
| + | [[Category: Hipolito, C J.]] | ||
| + | [[Category: Hirokane, R.]] | ||
| + | [[Category: Hirtake, J.]] | ||
| + | [[Category: Ikeguchi, K.]] | ||
| + | [[Category: Kato, H.]] | ||
| + | [[Category: Kimura, Y.]] | ||
| + | [[Category: Kodan, A.]] | ||
| + | [[Category: Nakatsu, T.]] | ||
| + | [[Category: Sakiyama, K.]] | ||
| + | [[Category: Suga, H.]] | ||
| + | [[Category: Ueda, K.]] | ||
| + | [[Category: Watanabe, B.]] | ||
| + | [[Category: Yamaguchi, T.]] | ||
| + | [[Category: Macrocyclic peptide]] | ||
| + | [[Category: Multi drug transporter]] | ||
| + | [[Category: Rec fold]] | ||
| + | [[Category: Transport protein-inhibitor complex]] | ||
Revision as of 07:48, 30 April 2014
Crystal structure of an inward-facing eukaryotic ABC multidrug transporter G277V/A278V/A279V mutant in complex with an cyclic peptide inhibitor, aCAP
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