2c3z: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2c3z.png|left|200px]]
-<!--
+==Crystal structure of a truncated variant of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus==
-The line below this paragraph, containing "STRUCTURE_2c3z", creates the "Structure Box" on the page.
+<StructureSection load='2c3z' size='340' side='right'caption='[[2c3z]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2c3z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C3Z FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2c3z|  PDB=2c3z  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3z OCA], [https://pdbe.org/2c3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c3z RCSB], [https://www.ebi.ac.uk/pdbsum/2c3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3z ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRPC_SACS2 TRPC_SACS2]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/2c3z_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=2c3z ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in the biosynthesis of tryptophan. It belongs to the large and versatile family of (betaalpha)(8)-barrel enzymes but has an unusual N-terminal extension of about 40 residues. Limited proteolysis with trypsin of IGPS from both Sulfolobus solfataricus (sIGPS) and Thermotoga maritima (tIGPS) removes about 25 N-terminal residues and one of the two extra helices contained therein. To assess the role of the extension, the N-terminally truncated variants sIGPSDelta(1-26) and tIGPSDelta(1-25) were produced recombinantly in Escherichia coli, purified, and characterized in comparison to the wild-type enzymes. Both sIGPSDelta(1-26) and tIGPSDelta(1-25) have unchanged oligomerization states and turnover numbers. In contrast, their Michaelis constants for the substrate 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate are increased, and their resistance toward unfolding induced by heat and guanidinium chloride is decreased. sIGPSDelta(1-26) was crystallized, and its X-ray structure was solved at 2.8 A resolution. The comparison with the known structure of sIGPS reveals small differences that account for its reduced substrate affinity and protein stability. The structure of the core of sIGPSDelta(1-26) is, however, unchanged compared to sIGPS, explaining its retained catalytic activity and consistent with the idea that it evolved from the same ancestor as the phosphoribosyl anthranilate isomerase and the alpha-subunit of tryptophan synthase. These (betaalpha)(8)-barrel enzymes catalyze the reactions preceding and following IGPS in tryptophan biosynthesis but lack an N-terminal extension.
-===CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS===
+Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity.,Schneider B, Knochel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R Biochemistry. 2005 Dec 20;44(50):16405-12. PMID:16342933<ref>PMID:16342933</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2c3z" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16342933}}, adds the Publication Abstract to the page
+*[[IGPS 3D structures|IGPS 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16342933 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16342933}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-C3Z is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C3Z OCA].
+[[Category: Saccharolobus solfataricus]]
+[[Category: Darimont B]]
-==Reference==
+[[Category: Dietrich S]]
-<ref group="xtra">PMID:16342933</ref><references group="xtra"/>
+[[Category: Hennig M]]
-[[Category: Indole-3-glycerol-phosphate synthase]]
+[[Category: Kirschner K]]
-[[Category: Sulfolobus solfataricus]]
+[[Category: Knoechel T]]
-[[Category: Darimont, B.]]
+[[Category: Schneider A]]
-[[Category: Dietrich, S.]]
+[[Category: Sterner R]]
-[[Category: Hennig, M.]]
-[[Category: Kirschner, K.]]
-[[Category: Knoechel, T.]]
-[[Category: Schneider, A.]]
-[[Category: Sterner, R.]]
-[[Category: Catalytic activity,divergent evolution,tryptophan biosynthesis,lyase,decarboxylase]]
-[[Category: Indole-3-glycerol phosphate synthase,protein stability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:42:43 2009''