Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP (Q27682108)

3

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Camilo Perez

object named as

Camilo Perez

1

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author name string

Caroline Koshy

2

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Christine Ziegler

The C-terminal domain of the betaine carrier BetP of Corynebacterium glutamicum is directly involved in sensing K+ as an osmotic stimulus

4

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language of work or name

English

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publication date

4 October 2012

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published in

Nature

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volume

490

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issue

7418

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page(s)

126-30

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cites work

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The osmoreactive betaine carrier BetP from Corynebacterium glutamicum is a sensor for cytoplasmic K+.

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Substrate specificity and ion coupling in the Na+/betaine symporter BetP

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X-ray structures of LeuT in substrate-free outward-open and apo inward-open states

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Molecular Basis of Alternating Access Membrane Transport by the Sodium-Hydantoin Transporter Mhp1

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Role of bundle helices in a regulatory crosstalk in the trimeric betaine transporter BetP.

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Conformational rearrangements to the intracellular open states of the LeuT and ApcT transporters are modulated by common mechanisms

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Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH.

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Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters

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Projection structure and oligomeric state of the osmoregulated sodium/glycine betaine symporter BetP of Corynebacterium glutamicum

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Regulatory properties and interaction of the C- and N-terminal domains of BetP, an osmoregulated betaine transporter from Corynebacterium glutamicum

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Locating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.

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Structural Asymmetry in a Trimeric Na+/Betaine Symporter, BetP, from Corynebacterium glutamicum

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Glycine betaine-assisted protein folding in a lysA mutant of Escherichia coli

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https://pubmed.ncbi.nlm.nih.gov/22940865

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The BCCT family of carriers: from physiology to crystal structure

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https://pubmed.ncbi.nlm.nih.gov/22940865

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Structure of a prokaryotic virtual proton pump at 3.2 Å resolution

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