2Y79
STRUCTURE OF THE FIRST GAF DOMAIN E87A MUTANT OF MYCOBACTERIUM TUBERCULOSIS DOSS
Summary for 2Y79
| Entry DOI | 10.2210/pdb2y79/pdb |
| Related | 2W3D 2W3E 2W3F 2W3G 2W3H |
| Descriptor | REDOX SENSOR HISTIDINE KINASE RESPONSE REGULATOR DEVS, PROTOPORPHYRIN IX CONTAINING FE, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | transferase |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Cellular location | Cytoplasm (Probable): P95194 |
| Total number of polymer chains | 2 |
| Total formula weight | 34761.06 |
| Authors | Cho, H.Y.,Cho, H.J.,Kang, B.S. (deposition date: 2011-01-30, release date: 2011-02-16, Last modification date: 2023-12-20) |
| Primary citation | Cho, H.Y.,Cho, H.J.,Kim, M.H.,Kang, B.S. Blockage of the Channel to Heme by the E87 Side Chain in the Gaf Domain of Mycobacterium Tuberculosis Doss Confers the Unique Sensitivity of Doss to Oxygen. FEBS Lett., 585:1873-, 2011 Cited by PubMed Abstract: Two sensor kinases, DosS and DosT, are responsible for recognition of hypoxia in Mycobacterium tuberculosis. Both proteins are structurally similar to each other, but DosS is a redox sensor while DosT binds oxygen. The primary difference between the two proteins is the channel to the heme present in their GAF domains. DosS has a channel that is blocked by E87 while DosT has an open channel. Absorption spectra of DosS mutants with an open channel show that they bind oxygen as DosT does when they are exposed to air, while DosT G85E mutant is oxidized similarly to DosS without formation of an oxy-ferrous form. This suggests that oxygen accessibility to heme is the primary factor governing the oxygen-binding properties of these proteins. PubMed: 21536032DOI: 10.1016/J.FEBSLET.2011.04.050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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