- PDB-2bm7: The Structure of MfpA (Rv3361c, P3221 Crystal form). The Pentapep... -
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Basic information
Entry
Database: PDB / ID: 2bm7
Title
The Structure of MfpA (Rv3361c, P3221 Crystal form). The Pentapeptide Repeat Protein from Mycobacterium tuberculosis Folds as A Right- handed Quadrilateral Beta-helix.
Components
PENTAPEPTIDE REPEAT FAMILY PROTEIN
Keywords
PENTAPEPTIDE REPEAT PROTEIN / FLUROQUINOLONE RESISTANCE / DNA GYRASE / DNA MIMICRY / RIGHT-HANDED QUADRILATERAL BETA-HELIX
Function / homology
Function and homology information
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) inhibitor activity / response to antibiotic / protein homodimerization activity Similarity search - Function
THE BIOLOGICALLY ACTIVE MOLECULE IS DIMERIC ANDTHE HEXAMERIC ASSEMBLY IS A TRIMER OF DIMERS. A BIOLOGICALLY ACTIVE DIMERIC ARRANGEMENT ISALSO OBSERVED IN A RELATED ENTRY 2BM4.
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Components
#1: Protein
PENTAPEPTIDEREPEATFAMILYPROTEIN / MFPA / RV3361C
Mass: 20325.859 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MYCOBACTERIUM TUBERCULOSIS (bacteria) / Strain: H37RV / Plasmid: PET28A / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O50390
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.5418 Å / Relative weight: 1
Reflection
Resolution: 2.7→30 Å / Num. obs: 16076 / % possible obs: 94 % / Observed criterion σ(I): 0 / Redundancy: 4.5 % / Biso Wilson estimate: 46.9 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 22.5
Reflection shell
Resolution: 2.7→2.8 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 6.3 / % possible all: 90.5
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Processing
Software
Name
Version
Classification
CNS
1
refinement
DENZO
datareduction
SCALEPACK
datascaling
AMoRE
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: PREVIOUS STRUCTURE DETERMINED BY SE-MET MAD Resolution: 2.7→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: MISSING RESIDUES FROM THE N AND C- TERMINI OF THE SUBMITTED COORDINATES AS COMPARED TO THE SUBMITTED SEQUENCE ARE REGIONS WHICH EXHIBITED NO ELECTRON DENSITY AND THEREFORE WERE NOT MODELED.
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