Unknown

Dataset Information

0

Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5?A resolution.

ABSTRACT: YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5?Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes.

SUBMITTER: Xu Q 

PROVIDER: S-EPMC2954210 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution.

Xu Qingping Q   McMullan Daniel D   Jaroszewski Lukasz L   Krishna S Sri SS   Elsliger Marc André MA   Yeh Andrew P AP   Abdubek Polat P   Astakhova Tamara T   Axelrod Herbert L HL   Carlton Dennis D   Chiu Hsiu Ju HJ   Clayton Thomas T   Duan Lian L   Feuerhelm Julie J   Grant Joanna J   Han Gye Won GW   Jin Kevin K KK   Klock Heath E HE   Knuth Mark W MW   Miller Mitchell D MD   Morse Andrew T AT   Nigoghossian Edward E   Okach Linda L   Oommachen Silvya S   Paulsen Jessica J   Reyes Ron R   Rife Christopher L CL   van den Bedem Henry H   Hodgson Keith O KO   Wooley John J   Deacon Ashley M AM   Godzik Adam A   Lesley Scott A SA   Wilson Ian A IA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20091027 Pt 10

YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes. ...[more]

Similar Datasets

Unknown High-resolution structure of RNase P protein from Thermotoga maritima.
| S-EPMC164615 | biostudies-literature
Unknown Structure of an essential GTPase, YsxC, from Thermotoga maritima.
| S-EPMC3107132 | biostudies-literature
Unknown Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution.
| S-EPMC1952466 | biostudies-literature
Unknown Structure of a periplasmic glucose-binding protein from Thermotoga maritima.
| S-EPMC3509965 | biostudies-literature
Unknown High-resolution structure of shikimate dehydrogenase from Thermotoga maritima reveals a tightly closed conformation.
| S-EPMC3887703 | biostudies-literature
Unknown Crystal structure of the cell division protein FtsA from Thermotoga maritima.
| S-EPMC313995 | biostudies-literature
Unknown Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima.
| S-EPMC1070373 | biostudies-literature
Unknown Cryo-EM Structure of Heterologous Protein Complex Loaded Thermotoga Maritima Encapsulin Capsid.
| S-EPMC7565527 | biostudies-literature
Unknown Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase.
| S-EPMC2792002 | biostudies-literature
Unknown The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.
| S-EPMC6839819 | biostudies-literature