|
|
| Line 1: |
Line 1: |
| [[Image:1svj.gif|left|200px]] | | {{Seed}} |
| | [[Image:1svj.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1svj| PDB=1svj | SCENE= }} | | {{STRUCTURE_1svj| PDB=1svj | SCENE= }} |
|
| |
|
| '''The solution structure of the nucleotide binding domain of KdpB'''
| | ===The solution structure of the nucleotide binding domain of KdpB=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| P-type ATPases are involved in the active transport of ions across biological membranes. The KdpFABC complex (P-type ATPase) of Escherichia coli is a high-affinity K+ uptake system that operates only when the cell experiences osmotic stress or K+ limitation. Here, we present the solution structure of the nucleotide binding domain of KdpB (backbone RMSD 0.17 A) and a model of the AMP-PNP binding mode based on intermolecular distance restraints. The calculated AMP-PNP binding mode shows the purine ring of the nucleotide to be "clipped" into the binding pocket via a pi-pi-interaction to F377 on one side and a cation-pi-interaction to K395 on the other. This binding mechanism seems to be conserved in all P-type ATPases, except the heavy metal transporting ATPases (type IB). Thus, we conclude that the Kdp-ATPase (currently type IA) is misgrouped and has more similarities to type III ATPases. The KdpB N-domain is the smallest and simplest known for a P-type ATPase, and represents a minimal example of this functional unit. No evidence of significant conformational changes was observed within the N-domain upon nucleotide binding, thus ruling out a role for ATP-induced conformational changes in the reaction cycle.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15364580}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15364580 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_15364580}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| 1SVJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVJ OCA]. | | 1SVJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVJ OCA]. |
|
| |
|
| ==Reference== | | ==Reference== |
| Line 29: |
Line 33: |
| [[Category: Kessler, H.]] | | [[Category: Kessler, H.]] |
| [[Category: Alpha-beta sandwich]] | | [[Category: Alpha-beta sandwich]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:34:17 2008'' |