Laminarase - Revision history

Alexander Berchansky at 13:25, 4 August 2022

Alexander Berchansky — Thu, 04 Aug 2022 13:25:47 GMT

←Older revision		Revision as of 13:25, 4 August 2022
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	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The <scene name='91/917928/Cv1/1'>oligosaccharide is bound at the concave face</scene> of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.	+	The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The <scene name='91/917928/Cv1/1'>oligosaccharide is bound at the concave face</scene> of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.

	==3D structures of laminarase==		==3D structures of laminarase==

Alexander Berchansky at 12:50, 4 August 2022

Alexander Berchansky — Thu, 04 Aug 2022 12:50:58 GMT

←Older revision		Revision as of 12:50, 4 August 2022
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	== Relevance ==		== Relevance ==

-	LAM cleaves laminarin which is an abundant polysaccharide found in alga which serves as carbon storage for nutrition of microbes. The depolymerization of laminarin initiates remineralization which is a key process in ocean biogeochemical cycles<ref>PMID:32917756</ref>.	+	LAM cleaves laminarin which is an abundant polysaccharide found in alga which serves as carbon storage for nutrition of microbes. The depolymerization of laminarin initiates remineralization which is a key process in ocean biogeochemical cycles<ref>PMID:32917756</ref>.

	== Structural highlights ==		== Structural highlights ==

-	The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The oligosaccharide is bound at the concave face of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.	+	The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The <scene name='91/917928/Cv1/1'>oligosaccharide is bound at the concave face</scene> of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.

	==3D structures of laminarase==		==3D structures of laminarase==

Alexander Berchansky at 12:46, 4 August 2022

Alexander Berchansky — Thu, 04 Aug 2022 12:46:45 GMT

←Older revision		Revision as of 12:46, 4 August 2022
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-	<StructureSection load='6xqf' size='340' side='right' caption='Laminarase complexed with cellotriose and Ca+2 (green) (PDB ID [[6xof]])' scene=''>	+	<StructureSection load='6xqf' size='340' side='right' caption='Laminarase complexed with cellotriose and Ca+2 (green) (PDB ID [[6xof]])' scene='91/917928/Cv/1'>

Michal Harel at 10:29, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 10:29:54 GMT

←Older revision		Revision as of 10:29, 21 July 2022
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	'''Laminarase''' (LAM) or '''endo-1,3-beta-glucanase family GH16''' or '''glycoside hydrolase family 16''' degrades 1,3-beta glycosyl linkages of beta-glucan via the hydrolysis of glycosidic bonds<ref>PMID:28900273</ref>.		'''Laminarase''' (LAM) or '''endo-1,3-beta-glucanase family GH16''' or '''glycoside hydrolase family 16''' degrades 1,3-beta glycosyl linkages of beta-glucan via the hydrolysis of glycosidic bonds<ref>PMID:28900273</ref>.
-
-	== Disease ==

	== Relevance ==		== Relevance ==
		+
		+	LAM cleaves laminarin which is an abundant polysaccharide found in alga which serves as carbon storage for nutrition of microbes. The depolymerization of laminarin initiates remineralization which is a key process in ocean biogeochemical cycles<ref>PMID:32917756</ref>.

	== Structural highlights ==		== Structural highlights ==

Michal Harel at 10:19, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 10:19:04 GMT

←Older revision		Revision as of 10:19, 21 July 2022
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	The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The oligosaccharide is bound at the concave face of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.		The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The oligosaccharide is bound at the concave face of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.
		+
		+	==3D structures of laminarase==
		+	[[Laminarase 3D structures]]
		+
	</StructureSection>		</StructureSection>
	== References ==		== References ==

Michal Harel at 10:17, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 10:17:30 GMT

←Older revision		Revision as of 10:17, 21 July 2022
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	== Structural highlights ==		== Structural highlights ==

-	~~This~~ is ~~a sample scene created~~ with ~~SAT to <scene name="~~/~~12/3456/Sample/1">color</scene> by Group,~~ and ~~another to make~~ <~~scene name="/12/3456/Sample/2"~~>~~a transparent representation~~</~~scene~~> ~~of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes~~.	+	The 3D structure of laminarase complexed with cellotriose shows the enzyme having a β-jellyroll fold typical to the GH16 family. The oligosaccharide is bound at the concave face of the molecule with 2 Glu residues defined as the nucleophile and acid/base residues in the active site. The ligand is coordinated via H-bonds and CH-π interactions<ref>PMID:33556371</ref>.
-		+
	</StructureSection>		</StructureSection>
	== References ==		== References ==

Michal Harel at 10:02, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 10:02:36 GMT

←Older revision		Revision as of 10:02, 21 July 2022
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-	<StructureSection load='6xqf' size='340' side='right' caption='~~Caption for this structure~~' scene=''>	+	<StructureSection load='6xqf' size='340' side='right' caption='Laminarase complexed with cellotriose and Ca+2 (green) (PDB ID [[6xof]])' scene=''>

Michal Harel at 09:26, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 09:26:17 GMT

←Older revision		Revision as of 09:26, 21 July 2022
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-	<StructureSection load='~~6m6p~~' size='340' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='6xqf' size='340' side='right' caption='Caption for this structure' scene=''>

Michal Harel at 09:23, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 09:23:42 GMT

←Older revision		Revision as of 09:23, 21 July 2022
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-	<StructureSection load='~~1stp~~' size='340' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='6m6p' size='340' side='right' caption='Caption for this structure' scene=''>

Michal Harel at 09:17, 21 July 2022

Michal Harel — Thu, 21 Jul 2022 09:17:57 GMT

←Older revision		Revision as of 09:17, 21 July 2022
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-
	<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>

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	== Function ==		== Function ==

-	'''Laminarase''' (LAM) or '''endo-1,3-beta-glucanase family GH16''' or '''glycoside hydrolase family ~~GH16~~''' degrades 1,3-beta glycosyl linkages of beta-glucan via the hydrolysis of glycosidic bonds<ref>PMID:28900273</ref>.	+	'''Laminarase''' (LAM) or '''endo-1,3-beta-glucanase family GH16''' or '''glycoside hydrolase family 16''' degrades 1,3-beta glycosyl linkages of beta-glucan via the hydrolysis of glycosidic bonds<ref>PMID:28900273</ref>.

	== Disease ==		== Disease ==