1N0E
CRYSTAL STRUCTURE OF A CELL DIVISION AND CELL WALL BIOSYNTHESIS PROTEIN UPF0040 FROM MYCOPLASMA PNEUMONIAE: INDICATION OF A NOVEL FOLD WITH A POSSIBLE NEW CONSERVED SEQUENCE MOTIF
Summary for 1N0E
Entry DOI | 10.2210/pdb1n0e/pdb |
Related | 1N0F 1N0G |
Descriptor | Protein mraZ (2 entities in total) |
Functional Keywords | cell division and cell wall biosynthesis protein, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, biosynthetic protein |
Biological source | Mycoplasma pneumoniae |
Total number of polymer chains | 8 |
Total formula weight | 154742.92 |
Authors | Chen, S.,Jancrick, J.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2002-10-13, release date: 2003-10-21, Last modification date: 2024-02-14) |
Primary citation | Chen, S.,Jancrick, J.,Yokota, H.,Kim, R.,Kim, S.-H. Crystal structure of a protein associated with cell division from Mycoplasma pneumoniae (GI: 13508053): a novel fold with a conserved sequence motif. Proteins, 55:785-791, 2004 Cited by PubMed Abstract: 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. PubMed: 15146477DOI: 10.1002/prot.10593 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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