PROSITE documentation PDOC51901Archaeal CBS proteins (ACP)-type metal binding (MB) domain profile
An archaeal family of CBS domain (see <PDOC51371>) proteins that are able to function as electron transfer proteins contains a small (~35 amino acids) C-terminal metal-binding (MB) domain containing four cysteine residues arranged in a Cys-X(2)-Cys-X(14-19)-Cys-X(1-4)-Cys motif. The archaeal CBS proteins (ACP)-type MB domain can bind several metals, with iron and zinc being the most abundant metals [1].
The ACP-type MB domain consists of three short β-strands forming a compact anti-parallel β-sheet that packs against the CBS domains (see PDB:1PVM>) [1].
The profile we developed covers the entire ACP-type MB domain.
Last update:August 2019 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Proudfoot M. Sanders S.A. Singer A. Zhang R. Brown G. Binkowski A. Xu L. Lukin J.A. Murzin A.G. Joachimiak A. Arrowsmith C.H. Edwards A.M. Savchenko A.V. Yakunin A.F. |
Title | Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. | |
Source | J. Mol. Biol. 375:301-315(2008). | |
PubMed ID | 18021800 | |
DOI | 10.1016/j.jmb.2007.10.060 |
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