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Crystal structure of a protein associated with cell division from Mycoplasma pneumoniae (GI: 13508053): A novel fold with a conserved sequence motif
Author(s) -
Chen Shengfeng,
Jancrick Jaru,
Yokota Hisao,
Kim Rosalind,
Kim SungHou
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10593
Subject(s) - threading (protein sequence) , mycoplasma pneumoniae , biology , crystal structure , protein structure , conserved sequence , homology (biology) , peptide sequence , structural genomics , chemistry , genetics , crystallography , amino acid , biochemistry , gene , history , archaeology , pneumonia
UPF0040 is a family of proteins implicated in a cellular function of bacteria cell division. There is no structure information available on protein of this family. We have determined the crystal structure of a protein from Mycoplasma pneumoniae that belongs to this family using X‐ray crystallography. Structural homology search reveals that this protein has a novel fold with no significant similarity to any proteins of known three‐dimensional structure. The crystal structures of the protein in three different crystal forms reveal that the protein exists as a ring of octamer. The conserved protein residues, including a highly conserved DXXXR motif, are examined on the basis of crystal structure. Proteins 2004. © 2004 Wiley‐Liss, Inc.