Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex (Record no. 48526)

MARC details
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fixed length control field 02260nam a2200301Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625153939.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-14332
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245 10 - TITLE STATEMENT
Title Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex
490 0# - SERIES STATEMENT
Volume/sequential designation Phil. Trans. R. Soc., 367(1592), p.1047-1058, 2012
520 3# - SUMMARY, ETC.
Summary, etc. Gram-negative bacteria frequently expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membranes. The three parts are the inner membrane, substrate-binding transporter (or pump); a periplasmic membrane fusion protein (MFP, or adaptor); and an outer membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. One such efflux system CusCBA is responsible for extruding biocidal Cu(I)and Ag(I)ions. We previously described the crystal structures of both the inner membrane transporter CusA and the MFP CusB of Escherichia coli.We also determined the co-crystal structure of the CusBA adaptor-transporter efflux complex, showing that the transporter CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. Here, we summarize the structural information of these efflux proteins, and present the accumulated evidence that this efflux system uses methionine residues to bind and export Cu(I)and Ag(I). Genetic and structural analyses suggest that the CusA pump is capable of picking up the metal ions from both the periplasm and the cytoplasm. We propose a stepwise shuttle mechanism for this pump to export metal ions from the cell.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element TRIPARTITE EFFLUX PUMP
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element MULTIDRUG RESISTANCE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element RESISTANCE-NODULATION-CELL DIVISION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element HEAVY-METAL EFFLUX
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element CUSCBA
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element X-RAY CRYSTALLOGRAPHY
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Long, Feng
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Su, C-C
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Lei, H-T
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Bolla, J.R.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Do, S.V.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Yu, E.W.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1-NsEqhP2-SO7L0P3f9cUT5dV4TbipOUO/view?usp=drivesdk">https://drive.google.com/file/d/1-NsEqhP2-SO7L0P3f9cUT5dV4TbipOUO/view?usp=drivesdk</a>
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Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-14332 25.06.2025 25.06.2025 Documentos solicitados