2NS1
Crystal structure of the e. coli ammonia channel AMTB complexed with the signal transduction protein GLNK
Summary for 2NS1
| Entry DOI | 10.2210/pdb2ns1/pdb |
| Related | 1GNK 1U7G 1XQF 2B2H 2GNK |
| Descriptor | Ammonia channel, Nitrogen regulatory protein P-II 2, octyl beta-D-glucopyranoside, ... (6 entities in total) |
| Functional Keywords | protein-protein complex, membrane protein, ammonia, channel, regulatory, inhibitor, signal protein, adp, bog, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, transport protein-signaling protein complex, transport protein/signaling protein |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P69681 |
| Total number of polymer chains | 2 |
| Total formula weight | 58521.21 |
| Authors | Gruswitz, F.,O'Connell III, J.,Stroud, R.M.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2006-11-02, release date: 2006-12-26, Last modification date: 2023-08-30) |
| Primary citation | Gruswitz, F.,O'Connell III, J.,Stroud, R.M. Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 Proc.Natl.Acad.Sci.USA, 104:42-47, 2007 Cited by PubMed Abstract: Ammonia conductance is highly regulated. A P(II) signal transduction protein, GlnK, is the final regulator of transmembrane ammonia conductance by the ammonia channel AmtB in Escherichia coli. The complex formed between AmtB and inhibitory GlnK at 1.96-A resolution shows that the trimeric channel is blocked directly by GlnK and how, in response to intracellular nitrogen status, the ability of GlnK to block the channel is regulated by uridylylation/deuridylylation at Y51. ATP and Mg(2+) augment the interaction of GlnK. The hydrolyzed product, adenosine 5'-diphosphate orients the surface of GlnK for AmtB blockade. 2-Oxoglutarate diminishes AmtB/GlnK association, and sites for 2-oxoglutarate are evaluated. PubMed: 17190799DOI: 10.1073/pnas.0609796104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.962 Å) |
Structure validation
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