We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

4c5l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='4c5l' size='340' side='right'caption='[[4c5l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='4c5l' size='340' side='right'caption='[[4c5l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4c5l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5L FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4c5l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5L FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PXL:3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE'>PXL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UEG:4,5-BIS(HYDROXYMETHYL)-2-METHYL-PYRIDIN-3-OL'>UEG</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PXL:3-HYDROXY-5-(HYDROXYMETHYL)-2-METHYLISONICOTINALDEHYDE'>PXL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UEG:4,5-BIS(HYDROXYMETHYL)-2-METHYL-PYRIDIN-3-OL'>UEG</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c5j|4c5j]], [[4c5k|4c5k]], [[4c5m|4c5m]], [[4c5n|4c5n]]</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=4c5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5l OCA], [https://pdbe.org/4c5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5l RCSB], [https://www.ebi.ac.uk/pdbsum/4c5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5l ProSAT]</span></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </span></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=4c5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5l OCA], [http://pdbe.org/4c5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c5l RCSB], [http://www.ebi.ac.uk/pdbsum/4c5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5l ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[[https://www.uniprot.org/uniprot/A0A0H3JTP0_STAAM A0A0H3JTP0_STAAM]]
-
Pyridoxal 5'-phosphate (PLP) is the active vitamer of vitamin B6 and acts as an essential cofactor in many aspects of amino acid and sugar metabolism. The virulence and survival of pathogenic bacteria such as Mycobacterium tuberculosis depend on PLP and deficiencies in humans have also been associated with neurological disorders and inflammation. While PLP can be synthesized by a de novo pathway in bacteria and plants, most higher organisms rely on a salvage pathway that phosphorylates either pyridoxal (PL) or its related vitamers, pyridoxine (PN) and pyridoxamine (PM). PL kinases (PLKs) are essential for this phosphorylation step and are thus of major importance for cellular viability. We recently identified a pyridoxal kinase (SaPLK) as a target of the natural product antibiotic rugulactone (Ru) in Staphylococcus aureus. Surprisingly, Ru selectively modified SaPLK not at the active site cysteine, but on a remote cysteine residue. Based on structural and biochemical studies, we now provide insight into an unprecedented dual Cys charge relay network that is mandatory for PL phosphorylation. The key component is the reactive Cys 110 residue in the lid region that forms a hemithioactetal intermediate with the 4 -aldehyde of PL. This hemithioacetal, in concert with the catalytic Cys 214, increases the nucleophilicity of the PL 5 -OH group for the inline displacement reaction with the g-phosphate of ATP. A closer inspection of related enzymes reveals that Cys 110 is conserved and thus serves as a characteristic mechanistic feature for a dual-function ribokinase subfamily herein termed CC-PLKs.
+
-
 
+
-
A sub-family of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage.,Nodwell MB, Koch MF, Alte F, Schneider S, Sieber SA J Am Chem Soc. 2014 Mar 6. PMID:24601602<ref>PMID:24601602</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4c5l" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Pyridoxal kinase|Pyridoxal kinase]]
*[[Pyridoxal kinase|Pyridoxal kinase]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Pyridoxal kinase]]
+
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
-
[[Category: Staam]]
+
[[Category: Alte F]]
-
[[Category: Alte, F]]
+
[[Category: Nodwell M]]
-
[[Category: Nodwell, M]]
+
[[Category: Schneider S]]
-
[[Category: Schneider, S]]
+
[[Category: Sieber SA]]
-
[[Category: Sieber, S A]]
+
-
[[Category: Ribokinase]]
+
-
[[Category: Transferase]]
+

Revision as of 17:28, 7 September 2022

Structure of the pyridoxal kinase from Staphylococcus aureus in complex with pyridoxal

PDB ID 4c5l

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/4c5l"
Personal tools