1FWP
| |
1EAY
| CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI | Descriptor: | CHEA, CHEY | Authors: | Mcevoy, M.M, Hausrath, A.C, Randolph, G.B, Remington, S.J, Dahlquist, F.W. | Deposit date: | 1998-04-23 | Release date: | 1998-07-15 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc.Natl.Acad.Sci.USA, 95, 1998
|
|
6WJE
| Copper resistance protein copG- Form 2 | Descriptor: | ACETATE ION, COPPER (II) ION, DUF411 domain-containing protein, ... | Authors: | Hausrath, A.C, Ly, A.T, McEvoy, M.M. | Deposit date: | 2020-04-13 | Release date: | 2020-06-24 | Last modified: | 2023-10-18 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | The bacterial copper resistance protein CopG contains a cysteine-bridged tetranuclear copper cluster. J.Biol.Chem., 295, 2020
|
|
5KU5
| |
1U8T
| Crystal structure of CheY D13K Y106W alone and in complex with a FliM peptide | Descriptor: | Chemotaxis protein cheY, Flagellar motor switch protein fliM, SULFATE ION | Authors: | Dyer, C.M, Quillin, M.L, Campos, A, Lu, J, McEvoy, M.M, Hausrath, A.C, Westbrook, E.M, Matsumura, P, Matthews, B.W, Dahlquist, F.W. | Deposit date: | 2004-08-06 | Release date: | 2004-10-05 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Structure of the Constitutively Active Double Mutant CheY(D13K Y106W) Alone and in Complex with a FliM Peptide J.Mol.Biol., 342, 2004
|
|
6WIS
| Copper resistance protein copG- Form 1 | Descriptor: | ACETATE ION, COPPER (II) ION, DUF411 domain-containing protein, ... | Authors: | Hausrath, A.C, Ly, A, McEvoy, M.M. | Deposit date: | 2020-04-10 | Release date: | 2020-06-24 | Last modified: | 2020-08-19 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | The bacterial copper resistance protein CopG contains a cysteine-bridged tetranuclear copper cluster. J.Biol.Chem., 295, 2020
|
|
1ZEQ
| 1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli | Descriptor: | Cation efflux system protein cusF | Authors: | Loftin, I.R, Franke, S, Roberts, S.A, Weichsel, A, Heroux, A, Montfort, W.R, Rensing, C, McEvoy, M.M. | Deposit date: | 2005-04-19 | Release date: | 2005-08-02 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | A Novel Copper-Binding Fold for the Periplasmic Copper Resistance Protein CusF. Biochemistry, 44, 2005
|
|
1C4W
| 1.9 A STRUCTURE OF A-THIOPHOSPHONATE MODIFIED CHEY D57C | Descriptor: | CHEMOTAXIS PROTEIN CHEY | Authors: | Halkides, C.J, McEvoy, M.M, Matsumura, P, Volz, K, Dahlquist, F.W. | Deposit date: | 1999-09-28 | Release date: | 2000-05-08 | Last modified: | 2023-12-27 | Method: | X-RAY DIFFRACTION (1.84 Å) | Cite: | The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry, 39, 2000
|
|
3SKX
| Crystal structure of the ATP binding domain of Archaeoglobus fulgidus COPB | Descriptor: | ACETATE ION, Copper-exporting P-type ATPase B | Authors: | Jayakanthan, S, Roberts, S.A, Weichsel, A, Arguello, J.M, McEvoy, M.M. | Deposit date: | 2011-06-23 | Release date: | 2012-06-20 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.59 Å) | Cite: | Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle. Biosci.Rep., 32, 2012
|
|
3SKY
| 2.1A crystal structure of the phosphate bound ATP binding domain of Archaeoglobus fulgidus COPB | Descriptor: | 3[N-MORPHOLINO]PROPANE SULFONIC ACID, Copper-exporting P-type ATPase B, PHOSPHATE ION | Authors: | Jayakanthan, S, Roberts, S.A, Weichsel, A, Arguello, J.M, McEvoy, M.M. | Deposit date: | 2011-06-23 | Release date: | 2012-06-20 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle. Biosci.Rep., 32, 2012
|
|