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

3EKI

Structural insights of the Mycoplasma hyorhinis protein Mh-p37: A putative thiamine pyrophosphate transporter

Summary for 3EKI
Entry DOI10.2210/pdb3eki/pdb
Related3E78 3E79
DescriptorHigh affinity transport system protein p37, THIAMINE DIPHOSPHATE, GLYCEROL, ... (6 entities in total)
Functional Keywordsmycoplasma, p37, tpp, cell membrane, lipoprotein, membrane, transport, transport protein, palmitate, extracytoplasmic thiamine binding lipoprotein, cypl, tpp binding protein
Biological sourceMycoplasma hyorhinis
Cellular locationCell membrane; Lipid-anchor: P15363
Total number of polymer chains1
Total formula weight47274.71
Authors
Sippel, K.H.,Robbins, A.H.,Reutzel, R.,McKenna, R. (deposition date: 2008-09-19, release date: 2009-06-23, Last modification date: 2023-08-30)
Primary citationSippel, K.H.,Robbins, A.H.,Reutzel, R.,Boehlein, S.K.,Namiki, K.,Goodison, S.,Agbandje-McKenna, M.,Rosser, C.J.,McKenna, R.
Structural insights into the extracytoplasmic thiamine-binding lipoprotein p37 of Mycoplasma hyorhinis
J.Bacteriol., 191:2585-2592, 2009
Cited by
PubMed Abstract: The Mycoplasma hyorhinis protein p37 has been implicated in tumorigenic transformation for more than 20 years. Though there are many speculations as to its function, based solely on sequence homology, the issue has remained unresolved. Presented here is the 1.6-A-resolution refined crystal structure of M. hyorhinis p37, renamed the extracytoplasmic thiamine-binding lipoprotein (Cypl). The structure shows thiamine pyrophosphate (TPP) and two calcium ions are bound to Cypl and give the first insights into possible functions of the Cypl-like family of proteins. Sequence alignments of Cypl-like proteins between several different species of mycoplasma show that the thiamine-binding site is likely conserved and structural alignments reveal the similarity of Cypl to various binding proteins. While the experimentally determined function of Cypl remains unknown, the structure shows that the protein is a TPP-binding protein, opening up many avenues for future mechanistic studies and making Cypl a possible target for combating mycoplasma infections and tumorigenic transformation.
PubMed: 19233924
DOI: 10.1128/JB.01680-08
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

245663

数据于2025-12-03公开中

PDB statisticsPDBj update infoContact PDBjnumon