1PA4

Solution structure of a putative ribosome-binding factor from Mycoplasma pneumoniae (MPN156)

Summary for 1PA4

• Entry DOI: 10.2210/pdb1pa4/pdb
• Related: 1KKG
• NMR Information: BMRB: 5796
• Descriptor: Probable ribosome-binding factor A (1 entity in total)
• Functional Keywords: ribosome-binding factor, structural genomics, distant homology, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, unknown function
• Biological source: Mycoplasma pneumoniae
• Cellular location: Cytoplasm (Potential): P75589
• Total number of polymer chains: 1
• Total formula weight: 13413.53

Authors

Rubin, S.M.,Pelton, J.G.,Yokota, H.,Kim, R.,Wemmer, D.E.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2003-05-13, release date: 2004-03-02, Last modification date: 2024-05-22)

Primary citation

Rubin, S.M.,Pelton, J.G.,Yokota, H.,Kim, R.,Wemmer, D.E.
Solution structure of a putative ribosome binding protein from Mycoplasma pneumoniae and comparison to a distant homolog.
J.STRUCT.FUNCT.GENOM., 4:235-243, 2003

PubMed Abstract: The solution structure of MPN156, a ribosome-binding factor A (RBFA) protein family member from Mycoplasma pneumoniae, is presented. The structure, solved by nuclear magnetic resonance, has a type II KH fold typical of RNA binding proteins. Despite only approximately 20% sequence identity between MPN156 and another family member from Escherichia coli, the two proteins have high structural similarity. The comparison demonstrates that many of the conserved residues correspond to conserved elements in the structures. Compared to a structure based alignment, standard alignment methods based on sequence alone mispair a majority of amino acids in the two proteins. Implications of these discrepancies for sequence based structural modeling are discussed.

PubMed: 15185964
DOI: 10.1023/B:JSFG.0000016127.57320.82

Experimental method

SOLUTION NMR