1cke
From Proteopedia
(New page: 200px<br /><applet load="1cke" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cke, resolution 1.75Å" /> '''CMP KINASE FROM ESCH...) |
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| - | [[Image:1cke.gif|left|200px]]<br /><applet load="1cke" size=" | + | [[Image:1cke.gif|left|200px]]<br /><applet load="1cke" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cke, resolution 1.75Å" /> | caption="1cke, resolution 1.75Å" /> | ||
'''CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME STRUCTURE'''<br /> | '''CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Background:. Nucleoside monophosphate kinases (NMP kinases) catalyze the | + | Background:. Nucleoside monophosphate kinases (NMP kinases) catalyze the reversible transfer of a phosphoryl group from a nucleoside triphosphate to a nucleoside monophosphate. Among them, cytidine monophosphate kinase from Escherichia coli has a striking particularity: it is specific for CMP, whereas in eukaryotes a unique UMP/CMP kinase phosphorylates both CMP and UMP with similar efficiency. Results:. The crystal structure of the CMP kinase apoenzyme from E. coli was solved by single isomorphous replacement and refined at 1.75 A resolution. The structure of the enzyme in complex with CDP was determined at 2.0 A resolution. Like other NMP kinases, the protein contains a central parallel beta sheet, the strands of which are connected by alpha helices. The enzyme differs from other NMP kinases in the presence of a 40-residue insert situated in the NMP-binding (NMPbind) domain. This insert contains two domains: one comprising a three-stranded antiparallel beta sheet, the other comprising two alpha helices. Conclusions:. Two features of the CMP kinase from E. coli have no equivalent in other NMP kinases of known structure. Firstly, the large NMPbind insert undergoes a CDP-induced rearrangement: its beta-sheet domain moves away from the substrate, whereas its helical domain comes closer to it in a motion likely to improve the protection of the active site. Secondly, residues involved in CDP recognition are conserved in CMP kinases and have no counterpart in other NMP kinases. The structures presented here are the first of a new family of NMP kinases specific for CMP. |
==About this Structure== | ==About this Structure== | ||
| - | 1CKE 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytidylate_kinase Cytidylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] Full crystallographic information is available from [http:// | + | 1CKE 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytidylate_kinase Cytidylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nucleotide monophosphate kinase]] | [[Category: nucleotide monophosphate kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:57 2008'' |
Revision as of 10:06, 21 February 2008
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CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME STRUCTURE
Overview
Background:. Nucleoside monophosphate kinases (NMP kinases) catalyze the reversible transfer of a phosphoryl group from a nucleoside triphosphate to a nucleoside monophosphate. Among them, cytidine monophosphate kinase from Escherichia coli has a striking particularity: it is specific for CMP, whereas in eukaryotes a unique UMP/CMP kinase phosphorylates both CMP and UMP with similar efficiency. Results:. The crystal structure of the CMP kinase apoenzyme from E. coli was solved by single isomorphous replacement and refined at 1.75 A resolution. The structure of the enzyme in complex with CDP was determined at 2.0 A resolution. Like other NMP kinases, the protein contains a central parallel beta sheet, the strands of which are connected by alpha helices. The enzyme differs from other NMP kinases in the presence of a 40-residue insert situated in the NMP-binding (NMPbind) domain. This insert contains two domains: one comprising a three-stranded antiparallel beta sheet, the other comprising two alpha helices. Conclusions:. Two features of the CMP kinase from E. coli have no equivalent in other NMP kinases of known structure. Firstly, the large NMPbind insert undergoes a CDP-induced rearrangement: its beta-sheet domain moves away from the substrate, whereas its helical domain comes closer to it in a motion likely to improve the protection of the active site. Secondly, residues involved in CDP recognition are conserved in CMP kinases and have no counterpart in other NMP kinases. The structures presented here are the first of a new family of NMP kinases specific for CMP.
About this Structure
1CKE is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Cytidylate kinase, with EC number 2.7.4.14 Full crystallographic information is available from OCA.
Reference
Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity., Briozzo P, Golinelli-Pimpaneau B, Gilles AM, Gaucher JF, Burlacu-Miron S, Sakamoto H, Janin J, Barzu O, Structure. 1998 Dec 15;6(12):1517-27. PMID:9862805
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