Garg, Saurabh K and Alam, Md Suhail and Bajpai, Richa and Kishan, K V Radha and Agrawal, Pushpa (2009) Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide. BMC biochemistry, 10. p. 1. ISSN 1471-2091
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Abstract
We conclude that M. tuberculosis GlgB has one intra-molecular disulfide bond which is formed between C193 and C617. WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB. For the first time, we report that GlgB is one of the in vivo substrate of M. tuberculosis WhiB1.
| Item Type: | Article |
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| Additional Information: | OPEN ACCESS |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 08 Dec 2011 19:36 |
| Last Modified: | 08 Jan 2015 09:39 |
| URI: | http://crdd.osdd.net/open/id/eprint/571 |
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