5sv9

<table><tr><td colspan='2'>[[5sv9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_2.2407 As 2.2407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SV9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5SV9 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5sv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sv9 OCA], [http://pdbe.org/5sv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sv9 RCSB], [http://www.ebi.ac.uk/pdbsum/5sv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sv9 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Bor1p is a secondary transporter in yeast that is responsible for boron transport. Bor1p belongs to the SLC4 family which controls in bicarbonate exchange and pH regulation in animals as well as borate uptake in plants. The SLC4 family is more distantly related to members of the Amino acid-Polyamine-organoCation (APC) superfamily, which includes well studied transporters such as LeuT, Mhp1, AdiC, vSGLT, UraA, SLC26Dg. Their mechanism generally involve relative movements of two domains: a core domain that binds substrate and a gate domain that in many cases mediates dimerization. In order to shed light on conformational changes governing transport by the SLC4 family, we grew helical membrane crystals of Bor1p from Saccharomyces mikatae and determined a structure at approximately 6 A resolution using cryo-electron microscopy. In order to evaluate the conformation of Bor1p in these crystals, a homology model was built based on the related anion exchanger from red blood cells (AE1). This homology model was fitted to the cryo-EM density map using the Molecular Dynamics (MD) Flexible Fitting method and then relaxed by all-atom MD simulation in explicit solvent and membrane. Mapping of water accessibility indicates that the resulting structure represents an inward-facing conformation. Comparisons of the resulting Bor1p model with the X-ray structure of AE1 in an outward-facing conformation, together with MD simulations of inward-facing and outward-facing Bor1p models, suggest rigid body movements of the core domain relative to the gate domain. These movements are consistent with the rocking-bundle transport mechanism described for other members of the APC superfamily. This article is protected by copyright. All rights reserved.

 

Structure of the SLC4 transporter Bor1p in an inward-facing conformation.,Coudray N, Seyler S, Lasala R, Zhang Z, Clark KM, Dumont ME, Rohou A, Beckstein O, Stokes DL Protein Sci. 2016 Oct 7. doi: 10.1002/pro.3061. PMID:27717063<ref>PMID:27717063</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<references/>

[[Category: As 2 2407]]

[[Category: Beckstein, O]]

[[Category: Clark, K M]]

[[Category: Coudray, N]]

[[Category: Dumont, M E]]

[[Category: Lasala, R]]

[[Category: Rohou, A]]

[[Category: Seyler, S]]

[[Category: Stokes, D L]]

[[Category: TEMIMPS, Transcontinental EM Initiative for Membrane Protein Structure]]

[[Category: Zhang, Z]]

[[Category: Transport protein]]