7cy4

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Crystal Structure of CMD1 in apo form

Structural highlights

7cy4 is a 1 chain structure with sequence from Chlamydomonas reinhardtii and Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:CIT, FE
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.CMD1_CHLRE Dioxygenase that catalyzes DNA modification by mediating the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-glyceryl-methylcytosine (5gmC) (PubMed:31043749, PubMed:33531488). Catalyzes the conjugation of a glyceryl moiety from L-ascorbate (vitamin C) to the methyl group of 5mC through a carbon-carbon bond (PubMed:31043749, PubMed:33531488). 5gmC DNA modification may be required during photosynthesis as an epigenetic mark that couteracts DNA methylation (PubMed:31043749).[1] [2]

References

  1. Xue JH, Chen GD, Hao F, Chen H, Fang Z, Chen FF, Pang B, Yang QL, Wei X, Fan QQ, Xin C, Zhao J, Deng X, Wang BA, Zhang XJ, Chu Y, Tang H, Yin H, Ma W, Chen L, Ding J, Weinhold E, Kohli RM, Liu W, Zhu ZJ, Huang K, Tang H, Xu GL. A vitamin-C-derived DNA modification catalysed by an algal TET homologue. Nature. 2019 May;569(7757):581-585. PMID:31043749 doi:10.1038/s41586-019-1160-0
  2. Li W, Zhang T, Sun M, Shi Y, Zhang XJ, Xu GL, Ding J. Molecular mechanism for vitamin C-derived C(5)-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1. Nat Commun. 2021 Feb 2;12(1):744. PMID:33531488 doi:10.1038/s41467-021-21061-2

Contents


PDB ID 7cy4

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