- PDB-3i38: Structure of a putative chaperone protein dnaj from klebsiella pn... -
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Basic information
Entry
Database: PDB / ID: 3i38
Title
Structure of a putative chaperone protein dnaj from klebsiella pneumoniae subsp. pneumoniae mgh 78578
Components
Putative chaperone DnaJ
Keywords
CHAPERONE / DNAJ / KLEBSIELLA PNEUMONIAE / STRUCTURAL GENOMICS / PSI-2 / Protein Structure Initiative / Midwest Center for Structural Genomics / MCSG
Function / homology
Function and homology information
bent DNA binding / nucleoid / chaperone cofactor-dependent protein refolding / unfolded protein binding / protein refolding / cytoplasm Similarity search - Function
AUTHORS HAD THE FOLLOWING COMMENTS ON THE SUPERHELICCAL STRUCTURE IN ASYMMETRIC UNIT: FIRST OF ALL, THE PROTEIN IS A SMALL PART OF A LARGE PROTEIN WHICH CONSISTS OF THREE DOMAINS. THEREFORE IT IS HARD TO PREDICT WHETHER THE FULL LENGTH PROTEIN WILL FORM A SIMILAR SUPERHELICAL STRUCTURE. LIGHT SCATTERING ANALYSIS CONFIRMS THAT THE PROTEIN DOMAIN FORMS A DIMER IN SOLUTION. AUTHORS ASSUME THAT THE SUPERHELICAL STRUCTURE IS AN ARTIFACT AND CREATED BY CRYSTAL PACKING. THIS IS THE VERY INTERESTING PATTERN BUT FROM FUNCTIONAL POINT OF VIEW WE DO NOT KNOW IF IT IS PHYSIOLOGICALLY RELEVANT.
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Components
#1: Protein
PutativechaperoneDnaJ
Mass: 11847.640 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Klebsiella pneumoniae subsp. pneumoniae MGH 78578 (bacteria) Gene: cbpA, KPN78578_44400, KPN_04509 / Plasmid: pMCSG19 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21Magic / References: UniProt: A6TH30
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