2mcm

From Proteopedia

MACROMOMYCIN

PDB ID 2mcm

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Structural highlights

2mcm is a 1 chain structure with sequence from "streptomyces_macromomyceticus"_hamada_and_okami "streptomyces macromomyceticus" hamada and okami. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MACM_STRMA] Binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of macromomycin, the apoprotein of the antitumor antibiotic auromomycin, has been determined and refined at 1.6-A resolution. The overall structure is composed of a flattened seven-stranded antiparallel beta-barrel and two antiparallel beta-sheet ribbons. The barrel and the ribbons define a deep cleft that is the chromophore binding site. The cleft is very accessible and in this structure is occupied by two 2-methyl-2,4-pentanediol and two water molecules. The overall shape of the binding site is similar to that of the analogue actinoxanthin. Highly specific side chains that are not conserved between different analogues extend into the binding site and may be important to the chromophore binding specificity.

Crystal structure analysis of auromomycin apoprotein (macromomycin) shows importance of protein side chains to chromophore binding selectivity.,Van Roey P, Beerman TA Proc Natl Acad Sci U S A. 1989 Sep;86(17):6587-91. PMID:2771945^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Van Roey P, Beerman TA. Crystal structure analysis of auromomycin apoprotein (macromomycin) shows importance of protein side chains to chromophore binding selectivity. Proc Natl Acad Sci U S A. 1989 Sep;86(17):6587-91. PMID:2771945