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.


5hu2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:16, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='5hu2' size='340' side='right'caption='[[5hu2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='5hu2' size='340' side='right'caption='[[5hu2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5hu2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans_r2 Anacystis nidulans r2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HU2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HU2 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5hu2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HU2 FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5htn|5htn]], [[5htj|5htj]], [[5htp|5htp]], [[5htr|5htr]], [[5htv|5htv]], [[5htx|5htx]], [[5hty|5hty]], [[5hux|5hux]], [[5hv7|5hv7]]</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]] 2.6&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Synpcc7942_2462 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1140 Anacystis nidulans R2])</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=5hu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hu2 OCA], [https://pdbe.org/5hu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hu2 RCSB], [https://www.ebi.ac.uk/pdbsum/5hu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hu2 ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hu2 OCA], [http://pdbe.org/5hu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hu2 RCSB], [http://www.ebi.ac.uk/pdbsum/5hu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hu2 ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/PSK_SYNE7 PSK_SYNE7] Exhibits ATP hydrolysis without substrate. Phosphorylates D-ribulose.<ref>PMID:27223615</ref>
-
The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana. Sequence alignment suggests that both kinases belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases. However, their exact physiological function and real substrates remain unknown. Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates. The two kinases exhibit nearly identical overall architecture, with both kinases possessing ATP hydrolysis activity in the absence of substrates. In addition, our enzymatic assays suggested that SePSK has the capability to phosphorylate D-ribulose. In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK. Using mutation and activity analysis, we further verified the key residues important for its catalytic activity. Moreover, our structural comparison with other family members suggests that there are major conformational changes in SePSK upon substrate binding, facilitating the catalytic process. Together, these results provide important information for a more detailed understanding of the cofactor and substrate binding mode as well as the catalytic mechanism of SePSK, and possible similarities with its plant homologue AtXK-1.
+
-
 
+
-
Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana.,Xie Y, Li M, Chang W PLoS One. 2016 May 25;11(5):e0156067. doi: 10.1371/journal.pone.0156067., eCollection 2016. PMID:27223615<ref>PMID:27223615</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5hu2" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Anacystis nidulans r2]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Chang, W]]
+
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
-
[[Category: Li, M]]
+
[[Category: Chang W]]
-
[[Category: Xie, Y]]
+
[[Category: Li M]]
-
[[Category: Mutation]]
+
[[Category: Xie Y]]
-
[[Category: Sugar kinase]]
+
-
[[Category: Synechococcus elongatus pcc7942-t11a]]
+
-
[[Category: Transferase]]
+

Current revision

Sugar kinases from Synechococcus elongatus PCC7942-T11A

PDB ID 5hu2

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/5hu2"
Personal tools