Guanylate kinase - Revision history

Michal Harel at 09:17, 21 July 2019

Michal Harel — Sun, 21 Jul 2019 09:17:13 GMT

←Older revision		Revision as of 09:17, 21 July 2019
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	</StructureSection>		</StructureSection>
-	==3D structures of guanylate kinase==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*Guanylate kinase
-
-	**[[6nui]] - hGK - human<br />
-	**[[1ex6]], [[4f4j]] – yGK – yeast<br />
-	**[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />
-	**[[1z8f]] – MtGK (mutant)<br />
-	**[[1s96]], [[2anc]] – EcGK – ''Escherichia coli''<br />
-	**[[1z6g]] – GK – ''Plasmodium falciparum''
-
-	*Guanylate kinase complex
-
-	**[[1lvg]] – mGK + ADP + GMP – mouse<br />
-	**[[1gky]], [[1ex7]] – yGK + GMP <br />
-	**[[2an9]] – EcGK + guanosine + GDP<br />
-	**[[2anb]] – EcGK + GMP<br />
-	**[[2f3t]] – EcGK + GMP derivative<br />
-	**[[2f3r]] – EcGK + adenosyl-guanosyl pentaphosphate<br />
-	**[[1znx]] – MtGK + GMP<br />
-	**[[1zny]], [[1znz]] – MtGK + GDP<br />
-	**[[2j41]] – SaGK + GMP – ''Staphylococcus aureus''<br />
-	**[[4qrh]] - SaGK + (P)PPGPP<br />
-	**[[2qor]] - GK + GMP – ''Plasmodium vivax''<br />
-	**[[3lnc]] - GK + GMP – ''Anaplasma phagocytophilum''<br />
-	**[[3tr0]] – GK residues 1-202 + GMP – ''Coxiella burnetii''<br />
-	**[[6mfu]] - GK + GMP + ADP – ''Cryprococcus neoformans''<br />
-
-	*Membrane-associated guanylate kinase WW and PDZ domain-containing protein 1; Domains – WW 295-388; PDZ1 455-580; PDZ3 640-721; PDZ4 839-922; PDZ6 1149-1233
-
-	**[[2kpk]] – hMAGI-1 PDZ1 – NMR<br />
-	**[[3bpu]] – hMAGI-1 PDZ3 (mutant) <br />
-	**[[2q9v]] - hMAGI-1 PDZ4 (mutant) <br />
-	**[[2r4h]] – hMAGI-1 PDZ6 (mutant) <br />
-	**[[2i04]] – hMAGI-1 PDZ1 + papillomavirus peptide<br />
-	**[[5n7d]], [[5n7f]], [[5n7g]] - hMAGI-1 PDZ1 + RSK1 peptide<br />
-	**[[2kpl]] – hMAGI-1 PDZ1 + protein E6 peptide - NMR<br />
-	**[[2ysd]], [[2yse]] – hMAGI-1 WW domain – NMR<br />
-	**[[2zaj]] – hMAGI-1 WW domain – NMR<br />
-	**[[5zys]] – mMAGI-1 PDZ4 + nephrin<br />
-
-	*Membrane-associated guanylate kinase inverted-2; Domains – PDZ1 454-564; PDZ2 642-724; PDZ3 802-981; PDZ4 943-1043; PDZ5 1169-1258
-
-	**[[1ueq]] – hMAGI-2 PDZ1 – NMR<br />
-	**[[1ujv]] – hMAGI-2 PDZ2 – NMR<br />
-	**[[1uep]] – hMAGI-2 PDZ3 – NMR<br />
-	**[[1uew]] – hMAGI-2 PDZ4 – NMR<br />
-	**[[1wfv]] – hMAGI-2 PDZ5 – NMR<br />
-
-	*Membrane-associated guanylate kinase WW and PDZ domain-containing protein 3
-
-	**[[3soe]] – hMAGI-3 PDZ3 residues 601-691<br />
-
-	}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 09:16, 21 July 2019

Michal Harel — Sun, 21 Jul 2019 09:16:06 GMT

←Older revision		Revision as of 09:16, 21 July 2019
Line 5:		Line 5:
	== Structural highlights ==		== Structural highlights ==
	The biological assembly of ''E. coli'' guanylate kinase is <scene name='48/487529/Cv/9'>homohexamer</scene>. The <scene name='48/487529/Cv/10'>GMP binding site</scene> of GK is <scene name='48/487529/Cv/8'>located between its nucleoside monophosphate-binding domain and the LID domain</scene><ref>PMID:16140325</ref>.		The biological assembly of ''E. coli'' guanylate kinase is <scene name='48/487529/Cv/9'>homohexamer</scene>. The <scene name='48/487529/Cv/10'>GMP binding site</scene> of GK is <scene name='48/487529/Cv/8'>located between its nucleoside monophosphate-binding domain and the LID domain</scene><ref>PMID:16140325</ref>.
		+
		+	==3D structures of guanylate kinase==
		+	[[Guanylate kinase 3D structures]]
		+
	</StructureSection>		</StructureSection>
	==3D structures of guanylate kinase==		==3D structures of guanylate kinase==
Line 13:		Line 17:
	*Guanylate kinase		*Guanylate kinase

		+	**[[6nui]] - hGK - human<br />
	**[[1ex6]], [[4f4j]] – yGK – yeast<br />		**[[1ex6]], [[4f4j]] – yGK – yeast<br />
	**[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />		**[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />
Line 19:		Line 24:
	**[[1z6g]] – GK – ''Plasmodium falciparum''		**[[1z6g]] – GK – ''Plasmodium falciparum''

-	*Guanylate kinase ~~binary~~ complex	+	*Guanylate kinase complex

		+	**[[1lvg]] – mGK + ADP + GMP – mouse<br />
	**[[1gky]], [[1ex7]] – yGK + GMP <br />		**[[1gky]], [[1ex7]] – yGK + GMP <br />
-	**[[1lvg]] – GK + ADP + GMP – mouse<br />
	**[[2an9]] – EcGK + guanosine + GDP<br />		**[[2an9]] – EcGK + guanosine + GDP<br />
	**[[2anb]] – EcGK + GMP<br />		**[[2anb]] – EcGK + GMP<br />
Line 33:		Line 38:
	**[[2qor]] - GK + GMP – ''Plasmodium vivax''<br />		**[[2qor]] - GK + GMP – ''Plasmodium vivax''<br />
	**[[3lnc]] - GK + GMP – ''Anaplasma phagocytophilum''<br />		**[[3lnc]] - GK + GMP – ''Anaplasma phagocytophilum''<br />
-	**[[3tr0]] – GK residues 1-202 + GMP – ''Coxiella burnetii''	+	**[[3tr0]] – GK residues 1-202 + GMP – ''Coxiella burnetii''<br />
		+	**[[6mfu]] - GK + GMP + ADP – ''Cryprococcus neoformans''<br />
		+
		+	*Membrane-associated guanylate kinase WW and PDZ domain-containing protein 1; Domains – WW 295-388; PDZ1 455-580; PDZ3 640-721; PDZ4 839-922; PDZ6 1149-1233
		+
		+	**[[2kpk]] – hMAGI-1 PDZ1 – NMR<br />
		+	**[[3bpu]] – hMAGI-1 PDZ3 (mutant) <br />
		+	**[[2q9v]] - hMAGI-1 PDZ4 (mutant) <br />
		+	**[[2r4h]] – hMAGI-1 PDZ6 (mutant) <br />
		+	**[[2i04]] – hMAGI-1 PDZ1 + papillomavirus peptide<br />
		+	**[[5n7d]], [[5n7f]], [[5n7g]] - hMAGI-1 PDZ1 + RSK1 peptide<br />
		+	**[[2kpl]] – hMAGI-1 PDZ1 + protein E6 peptide - NMR<br />
		+	**[[2ysd]], [[2yse]] – hMAGI-1 WW domain – NMR<br />
		+	**[[2zaj]] – hMAGI-1 WW domain – NMR<br />
		+	**[[5zys]] – mMAGI-1 PDZ4 + nephrin<br />
		+
		+	*Membrane-associated guanylate kinase inverted-2; Domains – PDZ1 454-564; PDZ2 642-724; PDZ3 802-981; PDZ4 943-1043; PDZ5 1169-1258
		+
		+	**[[1ueq]] – hMAGI-2 PDZ1 – NMR<br />
		+	**[[1ujv]] – hMAGI-2 PDZ2 – NMR<br />
		+	**[[1uep]] – hMAGI-2 PDZ3 – NMR<br />
		+	**[[1uew]] – hMAGI-2 PDZ4 – NMR<br />
		+	**[[1wfv]] – hMAGI-2 PDZ5 – NMR<br />
		+
		+	*Membrane-associated guanylate kinase WW and PDZ domain-containing protein 3

-	*~~Membrane~~-~~associated guanylate kinase~~	+	**[[3soe]] – hMAGI-3 PDZ3 residues 601-691<br />

-	**[[1uep]] – hMAGUK PDZ domain 3 – human – NMR<BR />
-	**[[1ueq]], [[2kpk]] - hMAGUK PDZ domain 1 – NMR<BR />
-	**[[1ujv]] - hMAGUK PDZ domain 2 – NMR<BR />
-	**[[3bpu]] - hMAGUK PDZ domain 3 (mutant)<br />
-	**[[3soe]] - hMAGUK PDZ domain 3<br />
-	**[[2q9v]] - hMAGUK PDZ domain 4<br />
-	**[[1uew]] - hMAGUK PDZ domain 4 – NMR<BR />
-	**[[1wfv]] - hMAGUK PDZ domain 5 – NMR<BR />
-	**[[2r4h]] - hMAGUK PDZ domain 6 (mutant)<br />
-	**[[2i04]] - hMAGUK PDZ domain 1 + papillomavirus peptide<br />
-	**[[2kpl]] - hMAGUK PDZ domain 1 + protein E6 peptide]] - NMR<BR />
-	**[[2ysd]], [[2yse]] - hMAGUK WW domain – NMR<BR />
-	**[[2zaj]] - hMAGUK WW 2 domain – NMR<BR />
	}}		}}
	== References ==		== References ==
	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]

Alexander Berchansky at 11:38, 4 April 2019

Alexander Berchansky — Thu, 04 Apr 2019 11:38:58 GMT

←Older revision		Revision as of 11:38, 4 April 2019
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 <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>.	+	The biological assembly of ''E. coli'' guanylate kinase is <scene name='48/487529/Cv/9'>homohexamer</scene>. The <scene name='48/487529/Cv/10'>GMP binding site</scene> of GK is <scene name='48/487529/Cv/8'>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==

Michal Harel at 09:31, 17 November 2016

Michal Harel — Thu, 17 Nov 2016 09:31:21 GMT

←Older revision		Revision as of 09:31, 17 November 2016
Line 14:		Line 14:

	**[[1ex6]], [[4f4j]] – yGK – yeast<br />		**[[1ex6]], [[4f4j]] – yGK – yeast<br />
-	**[[3sqk]] – yGK (mutant)<br />
	**[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />		**[[1s4q]], [[1znw]] – MtGK – ''Mycobacterium tuberculosis''<br />
	**[[1z8f]] – MtGK (mutant)<br />		**[[1z8f]] – MtGK (mutant)<br />

Alexander Berchansky at 08:44, 28 March 2016

Alexander Berchansky — Mon, 28 Mar 2016 08:44:03 GMT

←Older revision		Revision as of 08:44, 28 March 2016
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==

Alexander Berchansky at 08:18, 28 March 2016

Alexander Berchansky — Mon, 28 Mar 2016 08:18:42 GMT

←Older revision		Revision as of 08:18, 28 March 2016
Line 4:		Line 4:

	== Structural highlights ==		== Structural highlights ==
-	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 GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>.
	</StructureSection>		</StructureSection>
	==3D structures of guanylate kinase==		==3D structures of guanylate kinase==

Alexander Berchansky at 08:07, 28 March 2016

Alexander Berchansky — Mon, 28 Mar 2016 08:07:50 GMT

←Older revision		Revision as of 08:07, 28 March 2016
Line 1:		Line 1:
-	<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP ~~(stick model)~~, sulfate (PDB entry [[2anb]])' scene=''>	+	<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP, sulfate (PDB entry [[2anb]])' scene='48/487529/Cv/1'>
	== Function ==		== Function ==
	'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.		'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.

Michal Harel at 07:25, 20 March 2016

Michal Harel — Sun, 20 Mar 2016 07:25:16 GMT

←Older revision		Revision as of 07:25, 20 March 2016
Line 1:		Line 1:
-
	<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry [[2anb]])' scene=''>		<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry [[2anb]])' scene=''>
	== Function ==		== Function ==
-	'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP~~<ref>PMID:8528769</ref>~~. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.	+	'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.

	== Structural highlights ==		== Structural highlights ==
	The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>.		The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>.
-		+	</StructureSection>
	==3D structures of guanylate kinase==		==3D structures of guanylate kinase==

Michal Harel at 07:16, 20 March 2016

Michal Harel — Sun, 20 Mar 2016 07:16:24 GMT

←Older revision		Revision as of 07:16, 20 March 2016
Line 1:		Line 1:
-	{{STRUCTURE_1gky\| PDB=1gky \| SIZE=400\| SCENE= \|right\|CAPTION=Yeast guanylate kinase complex with GMP (stick model), sulfate and acetyl group [[1gky]] }}
-

		+	<StructureSection load='2anb' size='350' side='right' caption='E. coli guanylate kinase complex with GMP (stick model), sulfate (PDB entry [[2anb]])' scene=''>
		+	== Function ==
	'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP<ref>PMID:8528769</ref>. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.		'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP<ref>PMID:8528769</ref>. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.
		+
		+	== Structural highlights ==
		+	The GMP binding site of GK is located between its nucleoside monophosphate-binding domain and the LID domain<ref>PMID:16140325</ref>.

	==3D structures of guanylate kinase==		==3D structures of guanylate kinase==

Michal Harel at 12:12, 17 March 2016

Michal Harel — Thu, 17 Mar 2016 12:12:18 GMT

←Older revision		Revision as of 12:12, 17 March 2016
Line 1:		Line 1:
	{{STRUCTURE_1gky\| PDB=1gky \| SIZE=400\| SCENE= \|right\|CAPTION=Yeast guanylate kinase complex with GMP (stick model), sulfate and acetyl group [[1gky]] }}		{{STRUCTURE_1gky\| PDB=1gky \| SIZE=400\| SCENE= \|right\|CAPTION=Yeast guanylate kinase complex with GMP (stick model), sulfate and acetyl group [[1gky]] }}

-	~~<!--~~	+
-	~~Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.~~	+	'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP<ref>PMID:8528769</ref>. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it from an enzyme to a protein-binding GK domain<ref>PMID:21990344</ref>. The GK domain has no catalytic activity. The MAGUK contain PDZ (protein-protein interaction domain), WW (proline-rich interaction domain), SH3 (domain found in signaling pathway proteins) and GK domains.
-	~~Or use the four-green-boxes-button to insert scrollable text adjacent~~	+
-	~~to a Jmol applet. Check out the other buttons as well!~~	+
-	~~-->~~	+
-	'''Guanylate kinase''' (GK) catalyzes the transfer of phosphate from GMP to GDP using ATP as a phosphate source. GK is essential for recycling GMP and cGMP. GK also forms a domain in the membrane-associated GK (MAGUK) which functions in mitotic spindle orientation and cell adhesion. There is a single mutation in GK which converts it to a GK domain. The GK domain has no catalytic activity. The MAGUK contain PDZ, WW, SH3 and GK domains.	+

	==3D structures of guanylate kinase==		==3D structures of guanylate kinase==
Line 54:		Line 50:
	**[[2zaj]] - hMAGUK WW 2 domain – NMR<BR />		**[[2zaj]] - hMAGUK WW 2 domain – NMR<BR />
	}}		}}
		+	== References ==
		+	<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]