CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS

Insights Into the Inter-Ring Plasticity of Caseinolytic Proteases from the X-Ray Structure of Mycobacterium Tuberculosis Clpp1.

ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1

MSQVTDMRSNSQGLSLTDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYINSPGGSISAGMAIYDT
MVLAPCDIATYAMGMAASMGEFLLAAGTKGKRYALPHARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQ
PIERIEADSDRDRWFTAAEALEYGFVDHIITRAHVNGEAQ

STRUCTURE DETERMINED FROM COORDINATES OF SAME PROTEIN IN A DIFFERENT SPACE GROUP AT LOWER RESOLUTION

THE PROTEIN WAS CRYSTALLIZED BY THE SITTING DROP METHOD WITH 400NL PROTEIN PLUS 400NL MOTHERLIQUOR AND 100UL RESERVOIR. CONDITION WAS IDENTIFIED USING A SET OF RANDOM CONDITIONS GENERATED WITH CRYSTOOL SOFTWARE AND OPTIMIZED TO 9.576% (W/V) PEG 2000 0.2M LITHIUM SULFATE 0.1M MOPS (4-MORPHOLINEPROPANESULFONIC ACID) PH 6.5 WITH CRYSTOOL BY REDUCING THE PARAMETER SPACE TO THE REAGENTS UTILIZED. CRYSTALS SHOWED AFTER 2 DAYS

THE 3.0 A RESOLUTION STRUCTURE OF CASEINOLYTIC CLP PROTEASE 1 FROM MYCOBACTERIUM TUBERCULOSIS

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

CLPP ENDOPEPTIDASES ARE KNOWN TO BE
TETRADECAMERICAND THIS IS THE MULTIMERIC STATE FOUND
IN THISSTRUCTURE.HOWEVER, IN THIS PROTEIN, GEL
FILTRATION AND INTER-COMPLEX REGIONS BETWEEN THE
TWO HEPTAMERIC RINGS WOULDINDICATE THAT THE OLIGOMER
IS LIKELY TO BE HEPTAMERICIN SOLUTION.

SERINE PROTEASE, CLP PROTEASE, PROTEOLYTIC SUBUNIT, ENDOPEPTIDASE, MYCOBACTERIUM TUBERCULOSIS, ATP-DEPENDENT PROTEASE, HYDROLASE