1lk7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:16, 25 October 2023) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lk7.jpg|left|200px]]
 
-
{{Structure
+
==Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid==
-
|PDB= 1lk7 |SIZE=350|CAPTION= <scene name='initialview01'>1lk7</scene>, resolution 2.0&Aring;
+
<StructureSection load='1lk7' size='340' side='right'caption='[[1lk7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=DER:D-4-PHOSPHOERYTHRONIC ACID'>DER</scene>
+
<table><tr><td colspan='2'>[[1lk7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LK7 FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6]
+
</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&#8491;</td></tr>
-
|GENE=
+
<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=DER:D-4-PHOSPHOERYTHRONIC+ACID'>DER</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'>[https://proteopedia.org/fgij/fg.htm?mol=1lk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lk7 OCA], [https://pdbe.org/1lk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lk7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lk7 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RPIA_PYRHO RPIA_PYRHO]
 +
== 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/lk/1lk7_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=1lk7 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
A gene homologous to D-ribose-5-phosphate isomerase (EC 5.3.1.6) was found in the genome of Pyrococcus horikoshii. D-ribose-5-phosphate isomerase (PRI) is of particular metabolic importance since it catalyzes the interconversion between the ribose and ribulose forms involved in the pentose phosphate cycle and in the process of photosynthesis. The gene consisting of 687 bp was overexpressed in Escherichia coli, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C. The crystal structures of the enzyme, free and in complex with D-4-phosphoerythronic acid inhibitor, were determined. PRI is a tetramer in the crystal and in solution, and each monomer has a new fold consisting of two alpha/beta domains. The 3D structures and the characterization of different mutants indicate a direct or indirect catalytic role for the residues E107, D85, and K98.
-
'''Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid'''
+
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure.,Ishikawa K, Matsui I, Payan F, Cambillau C, Ishida H, Kawarabayasi Y, Kikuchi H, Roussel A Structure. 2002 Jun;10(6):877-86. PMID:12057201<ref>PMID:12057201</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1lk7" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
A gene homologous to D-ribose-5-phosphate isomerase (EC 5.3.1.6) was found in the genome of Pyrococcus horikoshii. D-ribose-5-phosphate isomerase (PRI) is of particular metabolic importance since it catalyzes the interconversion between the ribose and ribulose forms involved in the pentose phosphate cycle and in the process of photosynthesis. The gene consisting of 687 bp was overexpressed in Escherichia coli, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C. The crystal structures of the enzyme, free and in complex with D-4-phosphoerythronic acid inhibitor, were determined. PRI is a tetramer in the crystal and in solution, and each monomer has a new fold consisting of two alpha/beta domains. The 3D structures and the characterization of different mutants indicate a direct or indirect catalytic role for the residues E107, D85, and K98.
+
*[[Ribose-5-phosphate isomerase 3D structures|Ribose-5-phosphate isomerase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1LK7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK7 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure., Ishikawa K, Matsui I, Payan F, Cambillau C, Ishida H, Kawarabayasi Y, Kikuchi H, Roussel A, Structure. 2002 Jun;10(6):877-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12057201 12057201]
+
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
-
[[Category: Ribose-5-phosphate isomerase]]
+
[[Category: Cambillau C]]
-
[[Category: Single protein]]
+
[[Category: Ishida H]]
-
[[Category: Cambillau, C.]]
+
[[Category: Ishikawa K]]
-
[[Category: Ishida, H.]]
+
[[Category: Kawarabayasi Y]]
-
[[Category: Ishikawa, K.]]
+
[[Category: Kikuchi H]]
-
[[Category: Kawarabayasi, Y.]]
+
[[Category: Matsui I]]
-
[[Category: Kikuchi, H.]]
+
[[Category: Payan F]]
-
[[Category: Matsui, I.]]
+
[[Category: Roussel A]]
-
[[Category: Payan, F.]]
+
-
[[Category: Roussel, A.]]
+
-
[[Category: CL]]
+
-
[[Category: DER]]
+
-
[[Category: NA]]
+
-
[[Category: alpha/beta structure]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:48 2008''
+

Current revision

Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid

PDB ID 1lk7

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lk7"
Personal tools