3Q7K | pdb_00003q7k

Formate Channel FocA from Salmonella typhimurium

PDB DOI: https://doi.org/10.2210/pdb3Q7K/pdb

Classification: TRANSPORT PROTEIN
Organism(s): Salmonella enterica subsp. enterica serovar Typhi str. CT18
Expression System: Escherichia coli
Mutation(s): No
Membrane Protein: Yes OPMPDBTMMemProtMDmpstruc

Deposited: 2011-01-05 Released: 2011-04-27
Deposition Author(s): Lue, W., Du, J., Wacker, T., Gerbig-Smentek, E., Andrade, S.L.A., Einsle, O.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free:
0.254 (Depositor), 0.250 (DCC)
R-Value Work:
0.219 (Depositor), 0.220 (DCC)
R-Value Observed:
0.220 (Depositor)

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

pH-dependent gating in a FocA formate channel

Lu, W., Du, J., Wacker, T., Gerbig-Smentek, E., Andrade, S.L., Einsle, O.

(2011) Science 332: 352-354

PubMed: 21493860 Search on PubMed
DOI: https://doi.org/10.1126/science.1199098
Primary Citation of Related Structures:
3Q7K

PubMed Abstract:
The formate transporter FocA was described to switch its mode of operation from a passive export channel at high external pH to a secondary active formate/H(+) importer at low pH. The crystal structure of Salmonella typhimurium FocA at pH 4.0 shows that this switch involves a major rearrangement of the amino termini of individual protomers in the pentameric channel. The amino-terminal helices open or block transport in a concerted, cooperative action that indicates how FocA is gated in a pH-dependent way. Electrophysiological studies show that the protein acts as a specific formate channel at pH 7.0 and that it closes upon a shift of pH to 5.1.

Organizational Affiliation

Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany.

Macromolecule Content

Total Structure Weight: 321.22 kDa
Atom Count: 19,151
Modelled Residue Count: 2,523
Deposited Residue Count: 2,930
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Probable formate transporter	A B C D E A, B, C, D, E, F [auth G], G [auth H], H [auth I], I [auth J], J [auth K]	293	Salmonella enterica subsp. enterica serovar Typhi str. CT18	Mutation(s): 0 Gene Names: focA, STY0974, t1960 Membrane Entity: Yes
UniProt
Find proteins for Q7CQU0 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) Explore Q7CQU0 Go to UniProtKB: Q7CQU0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q7CQU0
Sequence Annotations Expand
Reference Sequence LOADING

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FMT Query on FMT Download Ideal Coordinates CCD File SDF format, chain R [auth H] SDF format, chain K [auth A] SDF format, chain L [auth B] SDF format, chain M [auth B] SDF format, chain N [auth C] SDF format, chain O [auth C] SDF format, chain P [auth D] SDF format, chain Q [auth H] SDF format, chain S [auth H] SDF format, chain T [auth I] SDF format, chain U [auth J] SDF format, chain V [auth K] SDF format, chain W [auth K] MOL2 format, chain R [auth H] MOL2 format, chain K [auth A] MOL2 format, chain L [auth B] MOL2 format, chain M [auth B] MOL2 format, chain N [auth C] MOL2 format, chain O [auth C] MOL2 format, chain P [auth D] MOL2 format, chain Q [auth H] MOL2 format, chain S [auth H] MOL2 format, chain T [auth I] MOL2 format, chain U [auth J] MOL2 format, chain V [auth K] MOL2 format, chain W [auth K] mmCIF format, chain R [auth H] mmCIF format, chain K [auth A] mmCIF format, chain L [auth B] mmCIF format, chain M [auth B] mmCIF format, chain N [auth C] mmCIF format, chain O [auth C] mmCIF format, chain P [auth D] mmCIF format, chain Q [auth H] mmCIF format, chain S [auth H] mmCIF format, chain T [auth I] mmCIF format, chain U [auth J] mmCIF format, chain V [auth K] mmCIF format, chain W [auth K]	K [auth A] L [auth B] M [auth B] N [auth C] O [auth C] K [auth A], L [auth B], M [auth B], N [auth C], O [auth C], P [auth D], Q [auth H], R [auth H], S [auth H], T [auth I], U [auth J], V [auth K], W [auth K]	FORMIC ACID C H₂ O₂ BDAGIHXWWSANSR-UHFFFAOYSA-N		Interactions Focus chain K [auth A] Focus chain L [auth B] Focus chain M [auth B] Focus chain N [auth C] Focus chain O [auth C] Focus chain P [auth D] Focus chain Q [auth H] Focus chain R [auth H] Focus chain S [auth H] Focus chain T [auth I] Focus chain U [auth J] Focus chain V [auth K] Focus chain W [auth K] Interactions & Density Focus chain K [auth A] Focus chain L [auth B] Focus chain M [auth B] Focus chain N [auth C] Focus chain O [auth C] Focus chain P [auth D] Focus chain Q [auth H] Focus chain R [auth H] Focus chain S [auth H] Focus chain T [auth I] Focus chain U [auth J] Focus chain V [auth K] Focus chain W [auth K]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.254 (Depositor), 0.250 (DCC)
R-Value Work: 0.219 (Depositor), 0.220 (DCC)
R-Value Observed: 0.220 (Depositor)

Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 105.951	α = 90
b = 205.723	β = 115.49
c = 106.046	γ = 90

Software Package:

Software Name	Purpose
MOLREP	phasing
REFMAC	refinement
MOSFLM	data reduction
SCALA	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-04-27

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2011-04-27
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2017-11-08
Changes: Refinement description
Version 1.3: 2023-11-01
Changes: Data collection, Database references, Derived calculations, Refinement description

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Help and Resources

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Formate Channel FocA from Salmonella typhimurium

pH-dependent gating in a FocA formate channel

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)

3Q7K | pdb_00003q7k