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1SUM

Crystal structure of a hypothetical protein at 2.0 A resolution

Summary for 1SUM
Entry DOI10.2210/pdb1sum/pdb
DescriptorPhosphate transport system protein phoU homolog 2, FE (III) ION, NICKEL (II) ION, ... (6 entities in total)
Functional Keywordsphou, abc transport, pst, structural genomics, berkeley structural genomics center, bsgc, structure funded by nih, protein structure initiative, psi, transport protein
Biological sourceThermotoga maritima
Cellular locationCytoplasm : Q9X256
Total number of polymer chains1
Total formula weight27498.82
Authors
Liu, J.,Lou, Y.,Yokota, H.,Adams, P.D.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2004-03-26, release date: 2004-08-24, Last modification date: 2024-11-13)
Primary citationLiu, J.,Lou, Y.,Yokota, H.,Adams, P.D.,Kim, R.,Kim, S.H.
Crystal structure of a PhoU protein homologue: a new class of metalloprotein containing multinuclear iron clusters.
J.Biol.Chem., 280:15960-15966, 2005
Cited by
PubMed Abstract: PhoU proteins are known to play a role in the regulation of phosphate uptake. In Thermotoga maritima, two PhoU homologues have been identified bioinformatically. Here we report the crystal structure of one of the PhoU homologues at 2.0 A resolution. The structure of the PhoU protein homologue contains a highly symmetric new structural fold composed of two repeats of a three-helix bundle. The structure unexpectedly revealed a trinuclear and a tetranuclear iron cluster that were found to be bound on the surface. Each of the two multinuclear iron clusters is coordinated by a conserved E(D)XXXD motif pair. Our structure reveals a new class of metalloprotein containing multinuclear iron clusters. The possible functional implication based on the structure are discussed.
PubMed: 15716271
DOI: 10.1074/jbc.M414117200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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