5x41

<StructureSection load='5x41' size='340' side='right' caption='[[5x41]], [[Resolution|resolution]] 3.47&Aring;' scene=''>

<table><tr><td colspan='2'>[[5x41]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X41 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x3x|5x3x]], [[5x40|5x40]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x41 OCA], [http://pdbe.org/5x41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x41 RCSB], [http://www.ebi.ac.uk/pdbsum/5x41 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x41 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/A0A0Q0R232_RHOCA A0A0Q0R232_RHOCA]] Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.[HAMAP-Rule:MF_01462]

Energy-coupling factor (ECF) transporters are a large family of ATP-binding cassette transporters recently identified in microorganisms. Responsible for micronutrient uptake from the environment, ECF transporters are modular transporters composed of a membrane substrate-binding component EcfS and an ECF module consisting of an integral membrane scaffold component EcfT and two cytoplasmic ATP binding/hydrolysis components EcfA/A'. ECF transporters are classified into groups I and II. Currently, the molecular understanding of group-I ECF transporters is very limited, partly due to a lack of transporter complex structural information. Here, we present structures and structure-based analyses of the group-I cobalt ECF transporter CbiMNQO, whose constituting subunits CbiM/CbiN, CbiQ, and CbiO correspond to the EcfS, EcfT, and EcfA components of group-II ECF transporters, respectively. Through reconstitution of different CbiMNQO subunits and determination of related ATPase and transporter activities, the substrate-binding subunit CbiM was found to stimulate CbiQO's basal ATPase activity. The structure of CbiMQO complex was determined in its inward-open conformation and that of CbiO in beta, gamma-methyleneadenosine 5'-triphosphate-bound closed conformation. Structure-based analyses revealed interactions between different components, substrate-gating function of the L1 loop of CbiM, and conformational changes of CbiO induced by ATP binding and product release within the CbiMNQO transporter complex. These findings enabled us to propose a working model of the CbiMNQO transporter, in which the transport process requires the rotation or toppling of both CbiQ and CbiM, and CbiN might function in coupling conformational changes between CbiQ and CbiM.Cell Research advance online publication 21 March 2017; doi:10.1038/cr.2017.38.

 

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== References ==

[[Category: Bao, Z]]

[[Category: Li, D]]

[[Category: Qi, X]]

[[Category: Zhang, P]]

[[Category: Zhao, W]]

[[Category: Cbimqo]]

[[Category: Ecf transporter]]

[[Category: Transport protein]]