1lu4

From Proteopedia
Jump to navigation Jump to search

1.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A SECRETED MYCOBACTERIUM TUBERCULOSIS DISULFIDE OXIDOREDUCTASE HOMOLOGOUS TO E. COLI DSBE: IMPLICATIONS FOR FUNCTIONS1.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A SECRETED MYCOBACTERIUM TUBERCULOSIS DISULFIDE OXIDOREDUCTASE HOMOLOGOUS TO E. COLI DSBE: IMPLICATIONS FOR FUNCTIONS

Structural highlights

1lu4 is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.12Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

MPT53_MYCTU Disulfide oxidoreductase that catalyzes the oxidation of reduced, unfolded secreted proteins to form disulfide bonds. Despite a weak homology to thioredoxin this cannot serve as a substrate for thioredoxin reductase.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, Eisenberg D. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. J Biol Chem. 2004 Jan 30;279(5):3516-24. Epub 2003 Nov 3. PMID:14597624 doi:10.1074/jbc.M311833200

1lu4, resolution 1.12Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA