User:Amer Ali/Sandbox 1 - Revision history

Amer Ali at 02:05, 30 April 2022

Amer Ali — Sat, 30 Apr 2022 02:05:57 GMT

←Older revision		Revision as of 02:05, 30 April 2022
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	== Function ==		== Function ==
-	TrpS is a pyridoxal 5’-phosphate (PLP)-dependent enzyme. TrpS has an alpha and beta chain that form a linear alpha-beta-beta-alpha heterotetrameric complex <ref name= "Michalska"> PMID: 31316809 </ref>. This is termed as the alpha2beta2 complex, and each subunit is also referred to as TrpA and TrpB for the alpha and beta subunits respectively. The alpha active site contains catalytic residues Glu and Asp, and a hydrophobic intramolecular tunnel allows for the transport of indole from the alpha subunit active site to the beta subunit active site (Miles ~~2001)~~. The alpha and beta chain are encoded by trpA and trpB genes that are involved in TrpS regulatory operon. In bacteria and plants, the alpha and beta chains are separate, but in fungi the two chains are fused into one protein (Tryptophan synthase, alpha chain, active site). The alpha2beta2 tetramer complex contains pyridoxal-phosphate, glycerol-3-phosphate, Na+ ions. Another key site in tryptophan synthase is the monovalent cation (MVC) site, which is made up of cations like Na+ and K+, along with Cs+ <ref name= "Dierkers"> DOI: 10.1021/bi9008374</ref> ~~<ref name= "Dunn"> DOI: 10.1007/978-1-4614-1533-6244 </ref> (Dunn, 2013)~~. For regulation, TrpA and TrpB cycle between low-activity open conformation and a high-activity closed state. This is done by the ~~bining~~ of an IGP substrate to TrpA which promotes the high activity closed state which activates the TrpB high activity closed state. The states are reset back to low activity open conformation by the production of L-Trp external aldimine <ref name= "Michalska"> PMID: 31316809 </ref>.	+	TrpS is a pyridoxal 5’-phosphate (PLP)-dependent enzyme. TrpS has an alpha and beta chain that form a linear alpha-beta-beta-alpha heterotetrameric complex <ref name= "Michalska"> PMID: 31316809 </ref>. This is termed as the alpha2beta2 complex, and each subunit is also referred to as TrpA and TrpB for the alpha and beta subunits respectively. The alpha active site contains catalytic residues Glu and Asp, and a hydrophobic intramolecular tunnel allows for the transport of indole from the alpha subunit active site to the beta subunit active site <ref name= "Miles"> DOI: 10.1002/tcr.4</ref>. The alpha and beta chain are encoded by trpA and trpB genes that are involved in TrpS regulatory operon. In bacteria and plants, the alpha and beta chains are separate, but in fungi the two chains are fused into one protein (Tryptophan synthase, alpha chain, active site). The alpha2beta2 tetramer complex contains pyridoxal-phosphate, glycerol-3-phosphate, Na+ ions. Another key site in tryptophan synthase is the monovalent cation (MVC) site, which is made up of cations like Na+ and K+, along with Cs+ <ref name= "Dierkers"> DOI: 10.1021/bi9008374</ref>. For regulation, TrpA and TrpB cycle between low-activity open conformation and a high-activity closed state. This is done by the binding of an IGP substrate to TrpA which promotes the high activity closed state which activates the TrpB high activity closed state. The states are reset back to low activity open conformation by the production of L-Trp external aldimine <ref name= "Michalska"> PMID: 31316809 </ref>.

Amer Ali at 02:01, 30 April 2022

Amer Ali — Sat, 30 Apr 2022 02:01:08 GMT

←Older revision		Revision as of 02:01, 30 April 2022
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-	==~~Your Heading Here (maybe something like 'Structure')~~==	+	== Tryptophan Synthase ==
-	<StructureSection load='~~1stp~~' size='340' side='right' caption='~~Caption for this~~ structure' scene=''>	+	<StructureSection load='1wbj' size='340' side='right' caption='Tryptophan synthase structure with alpha subunit (outer turqoise and light blue) and beta subunit (middle green and light green). Pyridoxal-phosphate, glycerol-3-phosphate, and Na+ ion shown within the structure (purple spheres) ' scene=''>
-	~~This is a default text for your page '''Amer Ali/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~	+
-	~~You may include any references to papers as~~ in~~: the use of JSmol in Proteopedia~~ <ref>DOI 10.~~1002~~/~~ijch~~.~~201300024~~</ref> or to the ~~article describing Jmol~~ <ref>~~PMID~~:~~21638687~~</ref> ~~to the rescue~~.	+	== Introduction ==
		+	Tryptophan synthase (TrpS) is an enzyme mainly found in bacteria, plants, and fungi <ref name= "Kulik"> DOI: 10.1016/j.jmb.2005.07.014 </ref>. TrpS must be functional for pathogenic bacteria in macrophages to survive, and it is used as a way to avoid host immune response. Tryptophan is necessary for bacteria and lower eukaryotic organisms for protein synthesis. Salmonella typhimurium and Escherichia coli serve as model organisms for the understanding of TrpS processes and structure <ref name= "Kulik"> DOI: 10.1016/j.jmb.2005.07.014 </ref>.

	== Function ==		== Function ==
		+	TrpS is a pyridoxal 5’-phosphate (PLP)-dependent enzyme. TrpS has an alpha and beta chain that form a linear alpha-beta-beta-alpha heterotetrameric complex <ref name= "Michalska"> PMID: 31316809 </ref>. This is termed as the alpha2beta2 complex, and each subunit is also referred to as TrpA and TrpB for the alpha and beta subunits respectively. The alpha active site contains catalytic residues Glu and Asp, and a hydrophobic intramolecular tunnel allows for the transport of indole from the alpha subunit active site to the beta subunit active site (Miles 2001). The alpha and beta chain are encoded by trpA and trpB genes that are involved in TrpS regulatory operon. In bacteria and plants, the alpha and beta chains are separate, but in fungi the two chains are fused into one protein (Tryptophan synthase, alpha chain, active site). The alpha2beta2 tetramer complex contains pyridoxal-phosphate, glycerol-3-phosphate, Na+ ions. Another key site in tryptophan synthase is the monovalent cation (MVC) site, which is made up of cations like Na+ and K+, along with Cs+ <ref name= "Dierkers"> DOI: 10.1021/bi9008374</ref> <ref name= "Dunn"> DOI: 10.1007/978-1-4614-1533-6244 </ref> (Dunn, 2013). For regulation, TrpA and TrpB cycle between low-activity open conformation and a high-activity closed state. This is done by the bining of an IGP substrate to TrpA which promotes the high activity closed state which activates the TrpB high activity closed state. The states are reset back to low activity open conformation by the production of L-Trp external aldimine <ref name= "Michalska"> PMID: 31316809 </ref>.
		+

	== Disease ==		== Disease ==

Amer Ali: New page: ==Your Heading Here (maybe something like 'Structure')== This is a default text for you...

Amer Ali — Sat, 30 Apr 2022 01:40:48 GMT

New page: ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for you...

New page

==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Amer Ali/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==

== Disease ==

== Relevance ==

== 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.

</StructureSection>
== References ==
<references/>