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2uyt

From Proteopedia

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Current revision

Structure of L-rhamnulose kinase in complex with ADP and beta-L- rhamnulose.

Structural highlights

2uyt is a 1 chain structure with sequence from Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.55Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RHAB_ECOUT Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). It could also play a role in the metabolism of some rare sugars such as L-fructose. Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. It can also phosphorylate L-fuculose and L-xylulose. It requires the R-configuration at the C-3 atom.[HAMAP-Rule:MF_01535]^[1]

Evolutionary Conservation

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

Publication Abstract from PubMed

The enzyme L-rhamnulose kinase from Escherichia coli participates in the degradation pathway of L-rhamnose, a common natural deoxy-hexose. The structure of the enzyme in a ternary complex with its substrates ADP and L-rhamnulose has been determined at 1.55A resolution and refined to R(cryst)/R(free) values of 0.179/0.209. The result was compared with the lower resolution structure of a corresponding complex containing L-fructose instead of L-rhamnulose. In light of the two established sugar positions and conformations, a number of rare sugars have been modeled into the active center of L-rhamnulose kinase and the model structures have been compared with the known enzymatic phosphorylation rates. Rare sugars are of rising interest for the synthesis of bioactive compounds.

Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures.,Grueninger D, Schulz GE FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Grueninger D, Schulz GE. Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures. FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582 doi:10.1016/j.febslet.2007.05.075
↑ Grueninger D, Schulz GE. Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures. FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582 doi:10.1016/j.febslet.2007.05.075

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2uyt"

Categories: Large Structures | Grueninger D | Schulz GE

@@ Line 3: / Line 3: @@
 <StructureSection load='2uyt' size='340' side='right'caption='[[2uyt]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2uyt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2UYT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2uyt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UYT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=LRH:6-DEOXY-BETA-L-FRUCTOFURANOSE'>LRH</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]] 1.55&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cgj|2cgj]], [[2cgk|2cgk]], [[2cgl|2cgl]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=LRH:6-DEOXY-BETA-L-FRUCTOFURANOSE'>LRH</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Rhamnulokinase Rhamnulokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.5 2.7.1.5] </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=2uyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyt OCA], [https://pdbe.org/2uyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uyt RCSB], [https://www.ebi.ac.uk/pdbsum/2uyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyt 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=2uyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uyt OCA], [http://pdbe.org/2uyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uyt RCSB], [http://www.ebi.ac.uk/pdbsum/2uyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uyt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RHAB_ECO57 RHAB_ECO57]] Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
+[https://www.uniprot.org/uniprot/RHAB_ECOUT RHAB_ECOUT] Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). It could also play a role in the metabolism of some rare sugars such as L-fructose. Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. It can also phosphorylate L-fuculose and L-xylulose. It requires the R-configuration at the C-3 atom.[HAMAP-Rule:MF_01535]<ref>PMID:17568582</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Ecobd]]
 [[Category: Large Structures]]
-[[Category: Rhamnulokinase]]
+[[Category: Grueninger D]]
-[[Category: Grueninger, D]]
+[[Category: Schulz GE]]
-[[Category: Schulz, G E]]
-[[Category: Hexokinase-hsp70-actin superfamily]]
-[[Category: In-line phosphoryl transfer]]
-[[Category: Induced fit]]
-[[Category: Kinase]]
-[[Category: L-rhamnulose kinase]]
-[[Category: Rare sugar]]
-[[Category: Rhamnose degradation]]
-[[Category: Rhamnose metabolism]]
-[[Category: Transferase]]

2uyt

From Proteopedia

Current revision

Structure of L-rhamnulose kinase in complex with ADP and beta-L- rhamnulose.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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