5ciq - Revision history

OCA at 07:21, 1 May 2024

OCA — Wed, 01 May 2024 07:21:53 GMT

←Older revision		Revision as of 07:21, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.65Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [https://pdbe.org/5ciq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [https://www.ebi.ac.uk/pdbsum/5ciq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ciq ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [https://pdbe.org/5ciq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [https://www.ebi.ac.uk/pdbsum/5ciq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ciq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>		[https://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Small GTPases regulate key processes in cells. Malfunction of their GTPase reaction by mutations is involved in severe diseases. Here, we compare the GTPase reaction of the slower hydrolyzing GTPase Ran with Ras. By combination of time-resolved FTIR-difference spectroscopy and QM/MM simulations we elucidate that the Mg2+ coordination by the phosphate groups, which varies largely among the X-ray structures, is the same for Ran and Ras. A new X-ray structure of a Ran.RanBD1 complex with improved resolution confirmed this finding and revealed a general problem with the refinement of Mg2+ in GTPases. The Mg2+ coordination is not responsible for the much slower GTPase reaction of Ran. Instead, the location of the Tyr39 side chain of Ran between the gamma-phosphate and Gln69 prevents the optimal positioning of the attacking water molecule by the Gln69 relative to the gamma-phosphate. This is confirmed in the RanY39A.RanBD1 crystal structure. The QM/MM simulations provide IR spectra of the catalytic center which agree very nicely with the experimental ones. The combination of both methods can correlate spectra with structure at atomic detail. For example the FTIR difference spectra of RasA18T and RanT25A mutants show that spectral differences are mainly due to the hydrogen bond of Thr25 to the alpha-phosphate in Ran. By integration of X-ray structure analysis, experimental and theoretical IR spectroscopy the catalytic center of the X-ray structural models are further refined to sub-Angstrom resolution, allowing an improved understanding of catalysis.
-
-	Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental and theoretical IR spectroscopy.,Rudack T, Jenrich S, Brucker S, Vetter IR, Gerwert K, Kotting C J Biol Chem. 2015 Aug 13. pii: jbc.M115.648071. PMID:26272610<ref>PMID:26272610</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5ciq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 12:07, 14 June 2023

OCA — Wed, 14 Jun 2023 12:07:57 GMT

←Older revision		Revision as of 12:07, 14 June 2023
Line 3:		Line 3:
	<StructureSection load='5ciq' size='340' side='right'caption='[[5ciq]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='5ciq' size='340' side='right'caption='[[5ciq]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAN, ARA24, OK/SW-cl.81 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [https://pdbe.org/5ciq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [https://www.ebi.ac.uk/pdbsum/5ciq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ciq ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [~~http~~://pdbe.org/5ciq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5ciq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5ciq ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN]] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>	+	[https://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brucker, S]]	+	[[Category: Brucker S]]
-	[[Category: Vetter~~, I R]]~~	+	[[Category: Vetter IR]]
-	~~[[Category: Gtpase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nuclear transport]]~~	+
-	~~[[Category: Transport protein~~]]	+

OCA at 11:40, 27 March 2020

OCA — Fri, 27 Mar 2020 11:40:26 GMT

←Older revision		Revision as of 11:40, 27 March 2020
Line 1:		Line 1:
		+
	==Ran GDP wild type tetragonal crystal form==		==Ran GDP wild type tetragonal crystal form==
-	<StructureSection load='5ciq' size='340' side='right' caption='[[5ciq]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='5ciq' size='340' side='right'caption='[[5ciq]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [http://pdbe.org/5ciq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [http://www.ebi.ac.uk/pdbsum/5ciq PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAN, ARA24, OK/SW-cl.81 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [http://pdbe.org/5ciq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [http://www.ebi.ac.uk/pdbsum/5ciq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ciq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5ciq" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5ciq" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[GTP-binding protein 3D structures\|GTP-binding protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Brucker, S]]		[[Category: Brucker, S]]
	[[Category: Vetter, I R]]		[[Category: Vetter, I R]]

OCA at 21:28, 15 October 2015

OCA — Thu, 15 Oct 2015 21:28:35 GMT

←Older revision		Revision as of 21:28, 15 October 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [http://www.ebi.ac.uk/pdbsum/5ciq PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [http://pdbe.org/5ciq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [http://www.ebi.ac.uk/pdbsum/5ciq PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 5ciq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:11, 9 September 2015

OCA — Wed, 09 Sep 2015 11:11:58 GMT

←Older revision		Revision as of 11:11, 9 September 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Ran GDP wild type tetragonal crystal form==
		+	<StructureSection load='5ciq' size='340' side='right' caption='[[5ciq]], [[Resolution\|resolution]] 1.65Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5ciq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CIQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ciq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ciq RCSB], [http://www.ebi.ac.uk/pdbsum/5ciq PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RAN_HUMAN RAN_HUMAN]] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref> Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.<ref>PMID:10400640</ref> <ref>PMID:8692944</ref> <ref>PMID:18591255</ref> <ref>PMID:18617507</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Small GTPases regulate key processes in cells. Malfunction of their GTPase reaction by mutations is involved in severe diseases. Here, we compare the GTPase reaction of the slower hydrolyzing GTPase Ran with Ras. By combination of time-resolved FTIR-difference spectroscopy and QM/MM simulations we elucidate that the Mg2+ coordination by the phosphate groups, which varies largely among the X-ray structures, is the same for Ran and Ras. A new X-ray structure of a Ran.RanBD1 complex with improved resolution confirmed this finding and revealed a general problem with the refinement of Mg2+ in GTPases. The Mg2+ coordination is not responsible for the much slower GTPase reaction of Ran. Instead, the location of the Tyr39 side chain of Ran between the gamma-phosphate and Gln69 prevents the optimal positioning of the attacking water molecule by the Gln69 relative to the gamma-phosphate. This is confirmed in the RanY39A.RanBD1 crystal structure. The QM/MM simulations provide IR spectra of the catalytic center which agree very nicely with the experimental ones. The combination of both methods can correlate spectra with structure at atomic detail. For example the FTIR difference spectra of RasA18T and RanT25A mutants show that spectral differences are mainly due to the hydrogen bond of Thr25 to the alpha-phosphate in Ran. By integration of X-ray structure analysis, experimental and theoretical IR spectroscopy the catalytic center of the X-ray structural models are further refined to sub-Angstrom resolution, allowing an improved understanding of catalysis.

-	~~The entry 5ciq is ON HOLD~~	+	Catalysis of GTP hydrolysis by small GTPases at atomic detail by integration of X-ray crystallography, experimental and theoretical IR spectroscopy.,Rudack T, Jenrich S, Brucker S, Vetter IR, Gerwert K, Kotting C J Biol Chem. 2015 Aug 13. pii: jbc.M115.648071. PMID:26272610<ref>PMID:26272610</ref>

-	~~Authors: Vetter~~, I.~~R., Brucker,~~ S.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Ran GDP wild type tetragonal crystal form~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Brucker, S]]		[[Category: Brucker, S]]
-	[[Category: Vetter, I.R]]	+	[[Category: Vetter, I R]]
		+	[[Category: Gtpase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nuclear transport]]
		+	[[Category: Transport protein]]

OCA: Protected "5ciq" [edit=sysop:move=sysop]

OCA — Wed, 22 Jul 2015 13:11:03 GMT

Protected "5ciq" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:11, 22 July 2015

OCA: New page: '''Unreleased structure''' The entry 5ciq is ON HOLD Authors: Vetter, I.R., Brucker, S. Description: Ran GDP wild type tetragonal crystal form Category: Unreleased Structures [[Cat...

OCA — Wed, 22 Jul 2015 13:11:02 GMT

New page: '''Unreleased structure''' The entry 5ciq is ON HOLD Authors: Vetter, I.R., Brucker, S. Description: Ran GDP wild type tetragonal crystal form Category: Unreleased Structures [[Cat...

New page

'''Unreleased structure'''

The entry 5ciq is ON HOLD

Authors: Vetter, I.R., Brucker, S.

Description: Ran GDP wild type tetragonal crystal form
[[Category: Unreleased Structures]]
[[Category: Brucker, S]]
[[Category: Vetter, I.R]]