1s6l Summary


Solution structure of MerB, the Organomercurial Lyase involved in the bacterial mercury resistance system

The structure was published by Di Lello, P., Benison, G.C., Valafar, H., et al., Summers, A.O., Legault, P., and Omichinski, J.G., in 2004 in a paper entitled "NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2004.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of Alkylmercury lyase. This molecule has the UniProt identifier P77072 (MERB_ECOLX)search. The sample contained 212 residues which is 100% of the natural sequence. Out of 212 residues 192 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Alkylmercury lyase P77072 (1-212) (MERB_ECOLX)search Escherichia colisearch 100% 212 90%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P77072 (1 - 212) Alkylmercury lyase Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P77072) MerB N-terminal domain-likesearch, MerB-likesearch "winged helix" repressor DNA binding domainsearch PF03243: Alkylmercury lyasesearch, PF12324: Helix-turn-helix domain of alkylmercury lyasesearch

Chain ID Biological process (GO) Molecular function (GO)
A (P77072) organomercury catabolic processsearch response to mercury ionsearch alkylmercury lyase activitysearch lyase activitysearch

Chain InterPro annotation
A Alkylmercury lyasesearch Winged helix-turn-helix DNA-binding domainsearch Alkylmercury lyase, helix-turn-helix domainsearch