1hpm
From Proteopedia
(New page: 200px<br /><applet load="1hpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hpm, resolution 1.70Å" /> '''HOW POTASSIUM AFFECT...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hpm.gif|left|200px]]<br /><applet load="1hpm" size=" | + | [[Image:1hpm.gif|left|200px]]<br /><applet load="1hpm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hpm, resolution 1.70Å" /> | caption="1hpm, resolution 1.70Å" /> | ||
'''HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE'''<br /> | '''HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystallographic anomalous scattering from potassium at 1.7 A resolution | + | Crystallographic anomalous scattering from potassium at 1.7 A resolution reveals two monovalent ions that interact with MgADP and P(i) in the nucleotide binding cleft of wild-type recombinant bovine Hsc70 ATPase fragment. K+ at site 1 interacts with oxygens of the beta-phosphate of ADP, whereas K+ at site 2 interacts with an oxygen of P(i). Both K+ ions also interact with specific H2O molecules in the first hydration shell of the octahedrally coordinated Mg2+ ion and with specific protein ligands. In crystals that have Na+ present, K+ is replaced by a Na+ ion at site 1 and by a Na(+)-H2O pair at site 2. The K+ ions are positioned where they could stabilize binding of a beta,gamma-bidentate MgATP complex with Hsc70, as well as a transition state during ATP hydrolysis, suggesting that monovalent ions act as specific metal cofactors in the ATPase reaction of Hsc70. |
==About this Structure== | ==About this Structure== | ||
| - | 1HPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, PO4, K, CL and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http:// | + | 1HPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPM OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Mckay, D | + | [[Category: Mckay, D B.]] |
| - | [[Category: Wilbanks, S | + | [[Category: Wilbanks, S M.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CL]] | [[Category: CL]] | ||
| Line 23: | Line 23: | ||
[[Category: hydrolase (acting on acid anhydrides)]] | [[Category: hydrolase (acting on acid anhydrides)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:39 2008'' |
Revision as of 11:03, 21 February 2008
|
HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE
Overview
Crystallographic anomalous scattering from potassium at 1.7 A resolution reveals two monovalent ions that interact with MgADP and P(i) in the nucleotide binding cleft of wild-type recombinant bovine Hsc70 ATPase fragment. K+ at site 1 interacts with oxygens of the beta-phosphate of ADP, whereas K+ at site 2 interacts with an oxygen of P(i). Both K+ ions also interact with specific H2O molecules in the first hydration shell of the octahedrally coordinated Mg2+ ion and with specific protein ligands. In crystals that have Na+ present, K+ is replaced by a Na+ ion at site 1 and by a Na(+)-H2O pair at site 2. The K+ ions are positioned where they could stabilize binding of a beta,gamma-bidentate MgATP complex with Hsc70, as well as a transition state during ATP hydrolysis, suggesting that monovalent ions act as specific metal cofactors in the ATPase reaction of Hsc70.
About this Structure
1HPM is a Single protein structure of sequence from Bos taurus with , , , and as ligands. Active as Adenosinetriphosphatase, with EC number 3.6.1.3 Full crystallographic information is available from OCA.
Reference
How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site., Wilbanks SM, McKay DB, J Biol Chem. 1995 Feb 3;270(5):2251-7. PMID:7836458
Page seeded by OCA on Thu Feb 21 13:03:39 2008
