Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1UWD

NMR STRUCTURE OF A PROTEIN WITH UNKNOWN FUNCTION FROM THERMOTOGA MARITIMA (TM0487), WHICH BELONGS TO THE DUF59 FAMILY.

Summary for 1UWD
Entry DOI10.2210/pdb1uwd/pdb
Related1WCJ
DescriptorHYPOTHETICAL PROTEIN TM0487 (1 entity in total)
Functional Keywordssimilar to paad protein, alpha/beta fold, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi, biosynthetic protein
Biological sourceTHERMOTOGA MARITIMA
Total number of polymer chains1
Total formula weight11517.34
Authors
Almeida, M.S.,Peti, W.,Herrmann, T.,Wuthrich, K. (deposition date: 2004-02-03, release date: 2004-12-14, Last modification date: 2024-05-15)
Primary citationAlmeida, M.S.,Herrmann, T.,Peti, W.,Wilson, I.A.,Wuthrich, K.
NMR Structure of the Conserved Hypothetical Protein Tm0487 from Thermotoga Maritima: Implications for 216 Homologous Duf59 Proteins.
Protein Sci., 14:2880-, 2005
Cited by
PubMed Abstract: The NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima represents an alpha/beta-topology formed by the regular secondary structures alpha1-beta1-beta2-alpha2-beta3-beta4-alpha3- beta5-3(10)-alpha4, with a small anti-parallel beta-sheet of beta-strands 1 and 2, and a mixed parallel/anti-parallel beta-sheet of beta-strands 3-5. Similar folds have previously been observed in other proteins, with amino acid sequence identity as low as 3% and a variety of different functions. There are also 216 sequence homologs of TM0487, which all have the signature sequence of domains of unknown function 59 (DUF59), for which no three-dimensional structures have as yet been reported. The TM0487 structure thus presents a platform for homology modeling of this large group of DUF59 proteins. Conserved among most of the DUF59s are 13 hydrophobic residues, which are clustered in the core of TM0487. A putative active site of TM0487 consisting of residues D20, E22, L23, T51, T52, and C55 is conserved in 98 of the 216 DUF59 sequences. Asp20 is buried within the proposed active site without any compensating positive charge, which suggests that its pK(a) value may be perturbed. Furthermore, the DUF59 family includes ORFs that are part of a conserved chromosomal group of proteins predicted to be involved in Fe-S cluster metabolism.
PubMed: 16199668
DOI: 10.1110/PS.051755805
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon