This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2jgp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:37, 9 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Structure of the TycC5-6 PCP-C bidomain of the tyrocidine synthetase TycC==
==Structure of the TycC5-6 PCP-C bidomain of the tyrocidine synthetase TycC==
-
<StructureSection load='2jgp' size='340' side='right' caption='[[2jgp]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+
<StructureSection load='2jgp' size='340' side='right'caption='[[2jgp]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
[[2jgp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JGP OCA]. <br>
+
<table><tr><td colspan='2'>[[2jgp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JGP FirstGlance]. <br>
-
<b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-
<b>[[Related_structure|Related:]]</b> [[1dny|1dny]]<br>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgp OCA], [https://pdbe.org/2jgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jgp RCSB], [https://www.ebi.ac.uk/pdbsum/2jgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jgp ProSAT]</span></td></tr>
-
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jgp RCSB], [http://www.ebi.ac.uk/pdbsum/2jgp PDBsum]</span><br>
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TYCC_BREPA TYCC_BREPA] Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
-
[[Image:Consurf_key_small.gif|right]]
+
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/2jgp_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/2jgp_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
-
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jgp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
The crystal structure of the bidomain PCP-C from modules 5 and 6 of the nonribosomal tyrocidine synthetase TycC was determined at 1.8 A resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of which is associated with the preceding peptidyl carrier protein (PCP) domain at its donor side. The relative arrangement of the PCP and the peptide bond-forming condensation (C) domain places the active sites approximately 50 A apart. Accordingly, this PCP-C structure represents a conformational state prior to peptide transfer from the donor-PCP to the acceptor-PCP domain, implying the existence of additional states of PCP-C domain interaction during catalysis. Additionally, PCP-C exerts a mode of cyclization activity that mimics peptide bond formation catalyzed by C domains. Based on mutational data and pK value analysis of active site residues, it is suggested that nonribosomal peptide bond formation depends on electrostatic interactions rather than on general acid/base catalysis.
The crystal structure of the bidomain PCP-C from modules 5 and 6 of the nonribosomal tyrocidine synthetase TycC was determined at 1.8 A resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of which is associated with the preceding peptidyl carrier protein (PCP) domain at its donor side. The relative arrangement of the PCP and the peptide bond-forming condensation (C) domain places the active sites approximately 50 A apart. Accordingly, this PCP-C structure represents a conformational state prior to peptide transfer from the donor-PCP to the acceptor-PCP domain, implying the existence of additional states of PCP-C domain interaction during catalysis. Additionally, PCP-C exerts a mode of cyclization activity that mimics peptide bond formation catalyzed by C domains. Based on mutational data and pK value analysis of active site residues, it is suggested that nonribosomal peptide bond formation depends on electrostatic interactions rather than on general acid/base catalysis.
Line 22: Line 26:
Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase.,Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO Structure. 2007 Jul;15(7):781-92. PMID:17637339<ref>PMID:17637339</ref>
Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase.,Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO Structure. 2007 Jul;15(7):781-92. PMID:17637339<ref>PMID:17637339</ref>
-
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2jgp" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 28: Line 34:
</StructureSection>
</StructureSection>
[[Category: Brevibacillus brevis]]
[[Category: Brevibacillus brevis]]
-
[[Category: Essen, L O.]]
+
[[Category: Large Structures]]
-
[[Category: Knappe, T A.]]
+
[[Category: Essen L-O]]
-
[[Category: Marahiel, M A.]]
+
[[Category: Knappe TA]]
-
[[Category: Samel, S A.]]
+
[[Category: Marahiel MA]]
-
[[Category: Schoenafinger, G.]]
+
[[Category: Samel SA]]
-
[[Category: Antibiotic biosynthesis]]
+
[[Category: Schoenafinger G]]
-
[[Category: Antibiotic]]
+
-
[[Category: Condensation domain]]
+
-
[[Category: Ligase]]
+
-
[[Category: Multifunctional enzyme]]
+
-
[[Category: Nonribosomal peptide synthetase]]
+
-
[[Category: Peptide bond formation]]
+
-
[[Category: Peptidyl carrier domain]]
+
-
[[Category: Phosphopantetheine]]
+
-
[[Category: Tyrocidine]]
+

Current revision

Structure of the TycC5-6 PCP-C bidomain of the tyrocidine synthetase TycC

PDB ID 2jgp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools