1IQS

Minimized average structure of MTH1880 from Methanobacterium Thermoautotrophicum

Summary for 1IQS

• Entry DOI: 10.2210/pdb1iqs/pdb
• Related: 1IQO
• NMR Information: BMRB: 5129
• Descriptor: MTH1880 (1 entity in total)
• Functional Keywords: alpha-beta, anti-parallel, metal binding protein
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 1
• Total formula weight: 9960.41

Authors

Lee, C.H.,Shin, J.,Bang, E.,Jung, J.W.,Yee, A.,Arrowsmith, C.H.,Lee, W. (deposition date: 2001-07-29, release date: 2002-07-29, Last modification date: 2023-12-27)

Primary citation

Lee, C.H.,Jung, J.W.,Yee, A.,Arrowsmith, C.H.,Lee, W.
Solution structure of a novel calcium binding protein, MTH1880, from Methanobacterium thermoautotrophicum.
Protein Sci., 13:1148-1154, 2004

PubMed Abstract: MTH1880 is a hypothetical protein from Methanobacterium thermoautotrophicum, a target organism of structural genomics. The solution structure determined by NMR spectroscopy demonstrates a typical alpha + beta-fold found in many proteins with different functions. The molecular surface of the protein reveals a small, highly acidic pocket comprising loop B (Asp36, Asp37, Asp38), the end of beta2 (Glu39), and loop D (Ser57, Ser58, Ser61), indicating that the protein would have a possible cation binding site. The NMR resonances of several amino acids within the acidic binding pocket in MTH1880, shifted upon addition of calcium ion. This calcium binding motif and overall topology of MTH1880 differ from those of other calcium binding proteins. MTH1880 did not show a calcium-induced conformational change typical of calcium sensor proteins. Therefore, we propose that the MTH1880 protein contains a novel motif for calcium-specific binding, and may function as a calcium buffering protein.

PubMed: 15044740
DOI: 10.1110/ps.03472104

Experimental method

SOLUTION NMR