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- PDB-3vyo: Crystal structure of Mycobacterium tuberculosis L,D-transpeptidas... -

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Basic information

Entry
Database: PDB / ID: 3vyo
TitleCrystal structure of Mycobacterium tuberculosis L,D-transpeptidase LdtMt2 N140 truncation mutant (resideus 140-408)
ComponentsProbable conserved lipoprotein LPPS
KeywordsTRANSFERASE / BETA BARREL / YkuD domain / L / D-transpeptidase / beta-lactam binding
Function / homology
Function and homology information


peptidoglycan-based cell wall biogenesis / peptidoglycan-protein cross-linking / peptidoglycan metabolic process / peptidoglycan L,D-transpeptidase activity / Transferases; Acyltransferases; Aminoacyltransferases / acyltransferase activity / peptidoglycan-based cell wall / cell wall organization / regulation of cell shape / extracellular region ...peptidoglycan-based cell wall biogenesis / peptidoglycan-protein cross-linking / peptidoglycan metabolic process / peptidoglycan L,D-transpeptidase activity / Transferases; Acyltransferases; Aminoacyltransferases / acyltransferase activity / peptidoglycan-based cell wall / cell wall organization / regulation of cell shape / extracellular region / metal ion binding / plasma membrane
Similarity search - Function
Immunoglobulin-like - #3710 / L,D-transpeptidase catalytic domain-like / L,D-transpeptidase catalytic domain-like / Bacterial Ig domain, transpeptidase-associated / Bacterial Ig domain / L,D-transpeptidase (L,D-TPase) catalytic domain profile. / L,D-transpeptidase catalytic domain / L,D-transpeptidase catalytic domain / L,D-transpeptidase catalytic domain-like / Prokaryotic membrane lipoprotein lipid attachment site profile. ...Immunoglobulin-like - #3710 / L,D-transpeptidase catalytic domain-like / L,D-transpeptidase catalytic domain-like / Bacterial Ig domain, transpeptidase-associated / Bacterial Ig domain / L,D-transpeptidase (L,D-TPase) catalytic domain profile. / L,D-transpeptidase catalytic domain / L,D-transpeptidase catalytic domain / L,D-transpeptidase catalytic domain-like / Prokaryotic membrane lipoprotein lipid attachment site profile. / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
L,D-transpeptidase 2 / L,D-transpeptidase 2
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.8 Å
AuthorsLi, W.J. / Li, D.F. / Bi, L.J. / Wang, D.C.
CitationJournal: Cell Res. / Year: 2013
Title: Crystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosis
Authors: Li, W.J. / Li, D.F. / Hu, Y.L. / Zhang, X.E. / Bi, L.J. / Wang, D.C.
History
DepositionSep 30, 2012Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 19, 2013Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Probable conserved lipoprotein LPPS
B: Probable conserved lipoprotein LPPS


Theoretical massNumber of molelcules
Total (without water)59,1242
Polymers59,1242
Non-polymers00
Water9,224512
1
A: Probable conserved lipoprotein LPPS


Theoretical massNumber of molelcules
Total (without water)29,5621
Polymers29,5621
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Probable conserved lipoprotein LPPS


Theoretical massNumber of molelcules
Total (without water)29,5621
Polymers29,5621
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1600 Å2
ΔGint-10 kcal/mol
Surface area21740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)116.370, 121.190, 122.990
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number24
Space group name H-MI212121

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Components

#1: Protein Probable conserved lipoprotein LPPS / L / D-transpeptidase


Mass: 29561.805 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN, residues 140-408
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Strain: H37Rv / Gene: Rv2518c / Plasmid: pMCSG7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3)
References: UniProt: O53223, UniProt: I6Y9J2*PLUS, EC: 2.3.2.12
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 512 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.67 Å3/Da / Density % sol: 66.46 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.2M magnesium acetate, 0.1M sodium cacodylate, 30% PEG8000 , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 98 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 0.97889 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 13, 2012
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97889 Å / Relative weight: 1
ReflectionResolution: 1.8→43.19 Å / Num. all: 80508 / Num. obs: 80508 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.5 % / Biso Wilson estimate: 20 Å2 / Rmerge(I) obs: 0.112 / Rsym value: 0.112 / Net I/σ(I): 9.8
Reflection shellResolution: 1.8→1.9 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.564 / Mean I/σ(I) obs: 2.7 / Num. unique all: 11575 / Rsym value: 0.564 / % possible all: 100

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SOLVEphasing
CNS1.2refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: SAD / Resolution: 1.8→42.27 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2249 4047 -RANDOM
Rwork0.2094 ---
obs0.2094 80435 99.9 %-
all-80508 --
Displacement parametersBiso mean: 26.1 Å2
Baniso -1Baniso -2Baniso -3
1-9.945 Å20 Å20 Å2
2---5.992 Å20 Å2
3----3.953 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.24 Å0.22 Å
Luzzati d res low-5 Å
Luzzati sigma a0.2 Å0.17 Å
Refinement stepCycle: LAST / Resolution: 1.8→42.27 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4007 0 0 512 4519
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.005014
X-RAY DIFFRACTIONc_angle_deg1.30668
X-RAY DIFFRACTIONc_dihedral_angle_d26.00557
X-RAY DIFFRACTIONc_improper_angle_d0.81852
LS refinement shellResolution: 1.8→1.91 Å
RfactorNum. reflection% reflection
Rfree0.292 649 -
Rwork0.268 --
obs-12603 100 %

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