5lhf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (18:25, 18 October 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Phosphoribosyl anthranilate isomerase from Thermococcus kodakaraensis==
==Phosphoribosyl anthranilate isomerase from Thermococcus kodakaraensis==
-
<StructureSection load='5lhf' size='340' side='right' caption='[[5lhf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+
<StructureSection load='5lhf' size='340' side='right'caption='[[5lhf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5lhf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHF FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5lhf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LHF FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribosylanthranilate_isomerase Phosphoribosylanthranilate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.24 5.3.1.24] </span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5lhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhf OCA], [http://pdbe.org/5lhf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhf RCSB], [http://www.ebi.ac.uk/pdbsum/5lhf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhf ProSAT]</span></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=5lhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhf OCA], [https://pdbe.org/5lhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lhf RCSB], [https://www.ebi.ac.uk/pdbsum/5lhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhf ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRPF_THEKO TRPF_THEKO]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
A phosphoribosyl anthranilate isomerase, TkTrpF, from Thermococcus kodakaraensis was expressed in Escherichia coli and purified to homogeneity. TkTrpF was crystallized and its structure was determined by molecular replacement in two different space groups (C2 and P1) using data to 1.85 and 1.75 A resolution, respectively. TkTrpF belongs to the class of TIM-barrel proteins. Structural comparison with other phosphoribosyl anthranilate isomerases (TrpFs) showed the highest structural similarity to Pyrococcus furiosus TrpF. Similarly to P. furiosus TrpF, TkTrpF is a monomer in solution, in contrast to other thermophilic enzymes, which exist as functional dimers. Although in space group P1 TkTrpF crystallizes with two molecules in the asymmetric unit, the interface is highly improbable in solution. Potential factors for the thermostability of TkTrpF were attributed to an increase in helical structure, an increased number of charged residues and an increase in the number of salt bridges.
 +
 +
Crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon Thermococcus kodakaraensis.,Perveen S, Rashid N, Papageorgiou AC Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):804-812. Epub 2016, Oct 24. PMID:27827353<ref>PMID:27827353</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5lhf" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Phosphoribosylanthranilate isomerase]]
+
[[Category: Large Structures]]
-
[[Category: Papageorgiou, A C]]
+
[[Category: Thermococcus kodakarensis KOD1]]
-
[[Category: Perveen, S]]
+
[[Category: Papageorgiou AC]]
-
[[Category: Rashid, N]]
+
[[Category: Perveen S]]
-
[[Category: Isomerase]]
+
[[Category: Rashid N]]
-
[[Category: Protein stability]]
+
-
[[Category: Tim barrel]]
+
-
[[Category: Tryptophan biosynthesis]]
+

Current revision

Phosphoribosyl anthranilate isomerase from Thermococcus kodakaraensis

PDB ID 5lhf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools