2.A.6.1.6
The Zn2+-specific exporter, ZneABC. The ZneB MFP plays an active role in substrate efflux through metal binding and release. Its 2.8 Å structure is available (De Angelis et al., 2010). 3.0 Å intermediate conformational structures of ZneA have been determined, revealing two Zn2+ binding sites separated by a channel, and the protein has been shown to catalyze electrogenic Zn2+:H+ antiport (Pak et al. 2013).
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| Accession Number: | Q1LCD9 |
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| Protein Name: | Heavy metal cation tricomponent efflux outer membrane porin ZneC (CzcC-like) |
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| Length: | 511 |
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| Molecular Weight: | 53838.00 |
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| Species: | Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [266264] |
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| Number of TMSs: | 3 |
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| Substrate |
zinc(2+), hydron |
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1: MAKITSISVA TLLALATAGC AVGPDFQRPA APETDRYTAT TLPAETASAS TPDGQAQRFA
61: PGQDVPAQWW TMFGSSELNA LVDAALRANP DLQAMEAALR VAQENVAAQR GAFFPSVDAS
121: YTPSRQKIAQ IIASPLSDNS DLFTLHTAQL SVSYVPDVFG GTRRQVESGV AQADVARFQW
181: QAAYLTLTSN VVNAAIQEAS LRAQIRATQD VIALSTRQLE AVRKQQRLGQ VGAAEVAAQE
241: ATLAQAEAAL PPLDRQLAQQ RNLLAALTGR LPSDAVPQQF EFEALTLPGT LPLSLPSRLV
301: GQRPDIRAAE AQMHAASAQI GVATAARLPN ITLTAALGSS SQAIGDLFTA GTGFWGISAG
361: LMQPIFKGGM LLHQQRAAEA AYKQASAQYR STVLTAYQGV ADALHAIEAD ARGLRTASDA
421: ERAAYRSFNI AQAQWKAGQI GYPAVMLAEQ TYRQSAITLV QARASRYSDT VGLMQALGGS
481: WEDEPGKTPE NQSDSKPAAA PEAVGKAQGN G