6sly - Revision history

OCA at 13:05, 1 March 2024

OCA — Fri, 01 Mar 2024 13:05:25 GMT

←Older revision		Revision as of 13:05, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>		<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>
-	</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).		[https://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Uniformly (13)C- and (15)N-labeled samples ensure fast and reliable nuclear magnetic resonance (NMR) assignments of proteins and are commonly used for structure elucidation by NMR. However, the preparation of uniformly labeled samples is a labor-intensive and expensive step. Reducing the portion of (13)C-labeled glucose by a factor of five using a fractional 20% (13)C- and 100% (15)N-labeling scheme could lower the total chemical costs, yet retaining sufficient structural information of uniformly [(13)C, (15)N]-labeled sample as a result of the improved sensitivity of NMR instruments. Moreover, fractional (13)C-labeling can facilitate reliable resonance assignments of sidechains because of the biosynthetic pathways of each amino-acid. Preparation of only one [20% (13)C, 100% (15)N]-labeled sample for small proteins (<15 kDa) could also eliminate redundant sample preparations of 100% (15)N-labeled and uniformly 100% [(13)C, (15)N]-labeled samples of proteins. We determined the NMR structures of a small alpha-helical protein, the C domain of IgG-binding protein A from Staphylococcus aureus (SpaC), and a small beta-sheet protein, CBM64 module using [20% (13)C, 100% (15)N]-labeled sample and compared with the crystal structures and the NMR structures derived from the 100% [(13)C, (15)N]-labeled sample. Our results suggest that one [20% (13)C, 100% (15)N]-labeled sample of small proteins could be routinely used as an alternative to conventional 100% [(13)C, (15)N]-labeling for backbone resonance assignments, NMR structure determination, (15)N-relaxation analysis, and ligand-protein interaction.
-
-	NMR Structure Determinations of Small Proteins Using only One Fractionally 20% (13)C- and Uniformly 100% (15)N-Labeled Sample.,Heikkinen HA, Backlund SM, Iwai H Molecules. 2021 Feb 1;26(3). pii: molecules26030747. doi:, 10.3390/molecules26030747. PMID:33535444<ref>PMID:33535444</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 6sly" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[TonB\|TonB]]		*[[TonB\|TonB]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:02, 14 June 2023

OCA — Wed, 14 Jun 2023 11:02:35 GMT

←Older revision		Revision as of 11:02, 14 June 2023
Line 3:		Line 3:
	<StructureSection load='6sly' size='340' side='right'caption='[[6sly]]' scene=''>		<StructureSection load='6sly' size='340' side='right'caption='[[6sly]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>
	</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>		</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/TONB_HELPY TONB_HELPY] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Uniformly (13)C- and (15)N-labeled samples ensure fast and reliable nuclear magnetic resonance (NMR) assignments of proteins and are commonly used for structure elucidation by NMR. However, the preparation of uniformly labeled samples is a labor-intensive and expensive step. Reducing the portion of (13)C-labeled glucose by a factor of five using a fractional 20% (13)C- and 100% (15)N-labeling scheme could lower the total chemical costs, yet retaining sufficient structural information of uniformly [(13)C, (15)N]-labeled sample as a result of the improved sensitivity of NMR instruments. Moreover, fractional (13)C-labeling can facilitate reliable resonance assignments of sidechains because of the biosynthetic pathways of each amino-acid. Preparation of only one [20% (13)C, 100% (15)N]-labeled sample for small proteins (<15 kDa) could also eliminate redundant sample preparations of 100% (15)N-labeled and uniformly 100% [(13)C, (15)N]-labeled samples of proteins. We determined the NMR structures of a small alpha-helical protein, the C domain of IgG-binding protein A from Staphylococcus aureus (SpaC), and a small beta-sheet protein, CBM64 module using [20% (13)C, 100% (15)N]-labeled sample and compared with the crystal structures and the NMR structures derived from the 100% [(13)C, (15)N]-labeled sample. Our results suggest that one [20% (13)C, 100% (15)N]-labeled sample of small proteins could be routinely used as an alternative to conventional 100% [(13)C, (15)N]-labeling for backbone resonance assignments, NMR structure determination, (15)N-relaxation analysis, and ligand-protein interaction.
		+
		+	NMR Structure Determinations of Small Proteins Using only One Fractionally 20% (13)C- and Uniformly 100% (15)N-Labeled Sample.,Heikkinen HA, Backlund SM, Iwai H Molecules. 2021 Feb 1;26(3). pii: molecules26030747. doi:, 10.3390/molecules26030747. PMID:33535444<ref>PMID:33535444</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6sly" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[TonB\|TonB]]		*[[TonB\|TonB]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Helicobacter pylori]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Ciragan A]]		[[Category: Ciragan A]]
	[[Category: Heikkinen HA]]		[[Category: Heikkinen HA]]
	[[Category: Iwai H]]		[[Category: Iwai H]]

OCA at 10:04, 17 February 2021

OCA — Wed, 17 Feb 2021 10:04:15 GMT

←Older revision		Revision as of 10:04, 17 February 2021
Line 1:		Line 1:

	==NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-285)==		==NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-285)==
-	<StructureSection load='6sly' size='340' side='right'caption='[[6sly~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='6sly' size='340' side='right'caption='[[6sly]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[6sly]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504].~~ Full ~~experimental~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EC544_07375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>	+	</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [https://pdbe.org/6sly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [https://www.ebi.ac.uk/pdbsum/6sly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [~~http~~://pdbe.org/6sly PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6sly PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[http://www.uniprot.org/uniprot/A0A438WSV6_HELPX A0A438WSV6_HELPX]] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.[RuleBase:RU362123]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The growing understanding of partially unfolded proteins increasingly points to their biological relevance in allosteric regulation, complex formation, and protein design. However, the structural characterization of disordered proteins remains challenging. NMR methods can access both the dynamics and structures of such proteins, yet suffering from a high degeneracy of NMR signals. Here, we overcame this bottleneck utilizing a salt-inducible split intein to produce segmentally isotope-labeled samples with the native sequence, including the ligation junction. With this technique, we investigated the NMR structure and conformational dynamics of TonB from Helicobacter pylori in the presence of a proline-rich low complexity region. Spin relaxation experiments suggest that the several nano-second time scale dynamics of the C-terminal domain (CTD) is almost independent of the faster pico-to-nanosecond dynamics of the low complexity central region (LCCR). Our results demonstrate the utility of segmental isotopic labeling for proteins with heterogenous dynamics such as TonB and could advance NMR studies of other partially unfolded proteins.

-	NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.,Ciragan A, Backlund SM, Mikula KM, Beyer HM, Samuli Ollila OH, Iwai H Front Chem. 2020 Mar 19;8:136. doi: 10.3389/fchem.2020.00136. eCollection 2020. PMID:32266203<ref>PMID:32266203</ref>	+	==See Also==
-		+	*[[TonB\|TonB]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 6sly" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 43504]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ciragan, A]]	+	[[Category: Ciragan A]]
-	[[Category: Heikkinen~~, H A~~]]	+	[[Category: Heikkinen HA]]
-	[[Category: Iwai, H]]	+	[[Category: Iwai H]]
-	~~[[Category: C-terminal domain]]~~	+
-	~~[[Category: Metal transport]]~~	+
-	~~[[Category: Tonb-dependent iron uptake~~]]	+

OCA at 07:17, 15 April 2020

OCA — Wed, 15 Apr 2020 07:17:13 GMT

←Older revision		Revision as of 07:17, 15 April 2020
Line 3:		Line 3:
	<StructureSection load='6sly' size='340' side='right'caption='[[6sly]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='6sly' size='340' side='right'caption='[[6sly]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6SLY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SLY FirstGlance]. <br>
-	</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [http://pdbe.org/6sly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [http://www.ebi.ac.uk/pdbsum/6sly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EC544_07375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [http://pdbe.org/6sly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [http://www.ebi.ac.uk/pdbsum/6sly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/A0A438WSV6_HELPX A0A438WSV6_HELPX]] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.[RuleBase:RU362123]		[[http://www.uniprot.org/uniprot/A0A438WSV6_HELPX A0A438WSV6_HELPX]] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.[RuleBase:RU362123]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The growing understanding of partially unfolded proteins increasingly points to their biological relevance in allosteric regulation, complex formation, and protein design. However, the structural characterization of disordered proteins remains challenging. NMR methods can access both the dynamics and structures of such proteins, yet suffering from a high degeneracy of NMR signals. Here, we overcame this bottleneck utilizing a salt-inducible split intein to produce segmentally isotope-labeled samples with the native sequence, including the ligation junction. With this technique, we investigated the NMR structure and conformational dynamics of TonB from Helicobacter pylori in the presence of a proline-rich low complexity region. Spin relaxation experiments suggest that the several nano-second time scale dynamics of the C-terminal domain (CTD) is almost independent of the faster pico-to-nanosecond dynamics of the low complexity central region (LCCR). Our results demonstrate the utility of segmental isotopic labeling for proteins with heterogenous dynamics such as TonB and could advance NMR studies of other partially unfolded proteins.
		+
		+	NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.,Ciragan A, Backlund SM, Mikula KM, Beyer HM, Samuli Ollila OH, Iwai H Front Chem. 2020 Mar 19;8:136. doi: 10.3389/fchem.2020.00136. eCollection 2020. PMID:32266203<ref>PMID:32266203</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6sly" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 43504]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Ciragan, A]]		[[Category: Ciragan, A]]

OCA at 10:18, 27 March 2020

OCA — Fri, 27 Mar 2020 10:18:37 GMT

←Older revision		Revision as of 10:18, 27 March 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6sly ~~is ON HOLD~~	+	==NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-285)==
-		+	<StructureSection load='6sly' size='340' side='right'caption='[[6sly]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
-	~~Authors~~: ~~Ciragan~~, A., ~~Heikkinen~~, H.A., ~~Iwai~~, H.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6sly]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SLY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SLY FirstGlance]. <br>
-	~~Description~~: ~~NMR solution structure~~ of ~~Helicobacter pylori TonB~~-~~CTD (residues 179-285)~~	+	</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=6sly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sly OCA], [http://pdbe.org/6sly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sly RCSB], [http://www.ebi.ac.uk/pdbsum/6sly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sly ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/A0A438WSV6_HELPX A0A438WSV6_HELPX]] Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.[RuleBase:RU362123]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Ciragan, A]]		[[Category: Ciragan, A]]
		+	[[Category: Heikkinen, H A]]
	[[Category: Iwai, H]]		[[Category: Iwai, H]]
-	[[Category: ~~Heikkinen, H.A~~]]	+	[[Category: C-terminal domain]]
		+	[[Category: Metal transport]]
		+	[[Category: Tonb-dependent iron uptake]]

OCA: Protected "6sly" [edit=sysop:move=sysop]

OCA — Wed, 28 Aug 2019 13:55:42 GMT

Protected "6sly" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:55, 28 August 2019

OCA: New page: '''Unreleased structure''' The entry 6sly is ON HOLD Authors: Ciragan, A., Heikkinen, H.A., Iwai, H. Description: NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-2...

OCA — Wed, 28 Aug 2019 13:55:40 GMT

New page: '''Unreleased structure''' The entry 6sly is ON HOLD Authors: Ciragan, A., Heikkinen, H.A., Iwai, H. Description: NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-2...

New page

'''Unreleased structure'''

The entry 6sly is ON HOLD

Authors: Ciragan, A., Heikkinen, H.A., Iwai, H.

Description: NMR solution structure of Helicobacter pylori TonB-CTD (residues 179-285)
[[Category: Unreleased Structures]]
[[Category: Ciragan, A]]
[[Category: Iwai, H]]
[[Category: Heikkinen, H.A]]