Guanylate kinase
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
| - | The biological assembly of ''E. coli'' guanylate kinase is <scene name='48/487529/Cv/2'>homohexamer</scene>. The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>. | + | The biological assembly of ''E. coli'' guanylate kinase is <scene name='48/487529/Cv/2'>homohexamer</scene>. The <scene name='48/487529/Cv/4'>GMP binding site</scene> of GK is <scene name='48/487529/Cv/5'>located between its nucleoside monophosphate-binding domain and the LID domain</scene><ref>PMID:16140325</ref>. |
</StructureSection> | </StructureSection> | ||
==3D structures of guanylate kinase== | ==3D structures of guanylate kinase== | ||
Revision as of 08:44, 28 March 2016
| |||||||||||
3D structures of guanylate kinase
Updated on 28-March-2016
References
- ↑ Johnston CA, Whitney DS, Volkman BF, Doe CQ, Prehoda KE. Conversion of the enzyme guanylate kinase into a mitotic-spindle orienting protein by a single mutation that inhibits GMP-induced closing. Proc Natl Acad Sci U S A. 2011 Nov 1;108(44):E973-8. Epub 2011 Oct 11. PMID:21990344 doi:10.1073/pnas.1104365108
- ↑ Hible G, Renault L, Schaeffer F, Christova P, Zoe Radulescu A, Evrin C, Gilles AM, Cherfils J. Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase. J Mol Biol. 2005 Oct 7;352(5):1044-59. PMID:16140325 doi:10.1016/j.jmb.2005.07.042
