1ank
From Proteopedia
(New page: 200px<br /><applet load="1ank" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ank, resolution 2.0Å" /> '''THE CLOSED CONFORMATI...) |
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| - | [[Image:1ank.gif|left|200px]]<br /><applet load="1ank" size=" | + | [[Image:1ank.gif|left|200px]]<br /><applet load="1ank" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ank, resolution 2.0Å" /> | caption="1ank, resolution 2.0Å" /> | ||
'''THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. CLOI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP'''<br /> | '''THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. CLOI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of E. coli adenylate kinase with bound AMP and AMPPNP at 2.0 | + | The structure of E. coli adenylate kinase with bound AMP and AMPPNP at 2.0 A resolution is presented. The protein crystallizes in space group C2 with two molecules in the asymmetric unit, and has been refined to an R factor of 20.1% and an Rfree of 31.6%. In the present structure, the protein is in the closed (globular) form with the large flexible lid domain covering the AMPPNP molecule. Within the protein, AMP and AMPPNP, and ATP analog, occupy the AMP and ATP sites respectively, which had been suggested by the most recent crystal structure of E. coli adenylate kinase with Ap5A bound (Muller and Schulz, 1992, ref. 1) and prior fluorescence studies (Liang et al., 1991, ref. 2). The binding of substrates and the positions of the active site residues are compared between the present structure and the E. coli adenylate kinase/Ap5A structure. We failed to detect a peak in the density map corresponding to the Mg2+ ion which is required for catalysis, and its absence has been attributed to the use of ammonium sulfate in the crystallization solution. Finally, a comparison is made between the present structure and the structure of the heavy chain of muscle myosin. |
==About this Structure== | ==About this Structure== | ||
| - | 1ANK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with AMP and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Full crystallographic information is available from [http:// | + | 1ANK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Berry, M | + | [[Category: Berry, M B.]] |
[[Category: Bilderback, T.]] | [[Category: Bilderback, T.]] | ||
[[Category: Glaser, M.]] | [[Category: Glaser, M.]] | ||
| - | [[Category: Jr., G | + | [[Category: Jr., G N.Phillips.]] |
[[Category: Liang, P.]] | [[Category: Liang, P.]] | ||
[[Category: Meador, B.]] | [[Category: Meador, B.]] | ||
| Line 24: | Line 24: | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:23 2008'' |
Revision as of 09:46, 21 February 2008
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THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. CLOI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP
Overview
The structure of E. coli adenylate kinase with bound AMP and AMPPNP at 2.0 A resolution is presented. The protein crystallizes in space group C2 with two molecules in the asymmetric unit, and has been refined to an R factor of 20.1% and an Rfree of 31.6%. In the present structure, the protein is in the closed (globular) form with the large flexible lid domain covering the AMPPNP molecule. Within the protein, AMP and AMPPNP, and ATP analog, occupy the AMP and ATP sites respectively, which had been suggested by the most recent crystal structure of E. coli adenylate kinase with Ap5A bound (Muller and Schulz, 1992, ref. 1) and prior fluorescence studies (Liang et al., 1991, ref. 2). The binding of substrates and the positions of the active site residues are compared between the present structure and the E. coli adenylate kinase/Ap5A structure. We failed to detect a peak in the density map corresponding to the Mg2+ ion which is required for catalysis, and its absence has been attributed to the use of ammonium sulfate in the crystallization solution. Finally, a comparison is made between the present structure and the structure of the heavy chain of muscle myosin.
About this Structure
1ANK is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Adenylate kinase, with EC number 2.7.4.3 Full crystallographic information is available from OCA.
Reference
The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP., Berry MB, Meador B, Bilderback T, Liang P, Glaser M, Phillips GN Jr, Proteins. 1994 Jul;19(3):183-98. PMID:7937733
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