Please use this identifier to cite or link to this item: https://doi.org/10.1002/prot.21126
DC FieldValue
dc.titleCrystal structure of uncleaved L-aspartate-α-decarboxylase from Mycobacterium tuberculosis
dc.contributor.authorGopalan, G.
dc.contributor.authorChopra, S.
dc.contributor.authorRanganathan, A.
dc.contributor.authorSwaminathan, K.
dc.date.accessioned2014-10-27T08:25:05Z
dc.date.available2014-10-27T08:25:05Z
dc.date.issued2006-12-01
dc.identifier.citationGopalan, G., Chopra, S., Ranganathan, A., Swaminathan, K. (2006-12-01). Crystal structure of uncleaved L-aspartate-α-decarboxylase from Mycobacterium tuberculosis. Proteins: Structure, Function and Genetics 65 (4) : 796-802. ScholarBank@NUS Repository. https://doi.org/10.1002/prot.21126
dc.identifier.issn08873585
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100372
dc.description.abstractL-aspartate-α-decarboxylase (ADC) is a critical regulatory enzyme in the pantothenate biosynthetic pathway and belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases. The expression level of ADC in Mycobacterium tuberculosis (Mtb) was confirmed by cDNA analysis, immunoblotting with an anti-ADC polyclonal antibody using whole cell lysate and immunoelectron microscopy. The recombinant ADC proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E. coli and the protein structure was determined at 2.99 Å resolution. The proteins fold into the double-ψ β-barrel structure. The subunits of the two tetramers (there are eight ADC molecules in the asymmetric unit) form pseudo four-fold rotational symmetry, similar to the E. coli ADC proenzyme structure. As pantothenate is synthesized in microorganisms, plants, and fungi but not in animals, structure elucidation of Mtb ADC is of substantial interest for structure-based drug development. © 2006 Wiley-Liss, Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/prot.21126
dc.sourceScopus
dc.subjectADC
dc.subjectCrystal structure
dc.subjectDrug target
dc.subjectL-aspartate-α- decarboxylase
dc.subjectMycobacterium tuberculosis
dc.subjectpanD gene
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1002/prot.21126
dc.description.sourcetitleProteins: Structure, Function and Genetics
dc.description.volume65
dc.description.issue4
dc.description.page796-802
dc.description.codenPSFGE
dc.identifier.isiut000242056500002
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

21
checked on Jun 29, 2020

WEB OF SCIENCETM
Citations

21
checked on Jun 22, 2020

Page view(s)

108
checked on Jun 27, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.