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<StructureSection load='1l2l' size='340' side='right'caption='[[1l2l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1l2l' size='340' side='right'caption='[[1l2l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1l2l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L2L FirstGlance]. <br>
<table><tr><td colspan='2'>[[1l2l]] is a 1 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=1L2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2L FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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]] 2&#8491;</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=1l2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2l OCA], [http://pdbe.org/1l2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l2l RCSB], [http://www.ebi.ac.uk/pdbsum/1l2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2l 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=1l2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2l OCA], [https://pdbe.org/1l2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2l RCSB], [https://www.ebi.ac.uk/pdbsum/1l2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GLKA_PYRHO GLKA_PYRHO]] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor.  
[https://www.uniprot.org/uniprot/GLKA_PYRHO GLKA_PYRHO] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1l2l 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=1l2l ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Although ATP is the most common phosphoryl group donor for kinases, some kinases from certain hyperthermophilic archaea such as Pyrococcus horikoshii and Thermococcus litoralis use ADP as the phosphoryl donor. Those are ADP-dependent glucokinases (ADPGK) and phosphofructokinases in their glycolytic pathway. Here, we succeeded in gene cloning the ADPGK from P. horikoshii OT3 (phGK) in Escherichia coli,and in easy preparation of the enzyme, crystallization, and the structure determination of the apo enzyme. Recently, the three-dimensional structure of the ADPGK from T. litoralis (tlGK) in a complex with ADP was reported. The overall structure of two homologous enzymes (56.7%) was basically similar: This means that they consisted of large alpha/beta-domains and small domains. However, a marked adjustment of the two domains, which is a 10-A translation and a 20 degrees rotation from the conserved GG sequence located at the center of the hinge, was observed between the apo-phGK and ADP-tlGK structures. The ADP-binding loop (430-439) was disordered in the apo form. It is suggested that a large conformational change takes place during the enzymatic reaction.
Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase.,Tsuge H, Sakuraba H, Kobe T, Kujime A, Katunuma N, Ohshima T Protein Sci. 2002 Oct;11(10):2456-63. PMID:12237466<ref>PMID:12237466</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1l2l" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hexokinase|Hexokinase]]
*[[Hexokinase 3D structures|Hexokinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrococcus shinkaii]]
[[Category: Glucokinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Katunuma, N]]
[[Category: Pyrococcus horikoshii]]
[[Category: Ohshima, T]]
[[Category: Katunuma N]]
[[Category: Sakuraba, H]]
[[Category: Ohshima T]]
[[Category: Tsuge, H]]
[[Category: Sakuraba H]]
[[Category: Adp glucokinase apo]]
[[Category: Tsuge H]]
[[Category: Transferase]]

Latest revision as of 16:26, 13 March 2024

Crystal structure of ADP-dependent glucokinase from a Pyrococcus HorikoshiiCrystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii

Structural highlights

1l2l is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLKA_PYRHO Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1l2l, resolution 2.00Å

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OCA
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