7zd4: Difference between revisions
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New page: '''Unreleased structure''' The entry 7zd4 is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ions== | |||
<StructureSection load='7zd4' size='340' side='right'caption='[[7zd4]], [[Resolution|resolution]] 2.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7zd4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZD4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=7zd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zd4 OCA], [https://pdbe.org/7zd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zd4 RCSB], [https://www.ebi.ac.uk/pdbsum/7zd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zd4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SAHH_PSEAE SAHH_PSEAE] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report biochemical and structural studies on inhibiting bacterial S-adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor. | |||
A closer look at molecular mechanisms underlying inhibition of S-adenosyl-L-homocysteine hydrolase by transition metal cations.,Gawel M, Malecki PH, Sliwiak J, Stepniewska M, Imiolczyk B, Czyrko-Horczak J, Jakubczyk D, Marczak L, Plonska-Brzezinska ME, Brzezinski K Chem Commun (Camb). 2024 Oct 8;60(81):11504-11507. doi: 10.1039/d4cc03143a. PMID:39230573<ref>PMID:39230573</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7zd4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa PAO1]] | |||
[[Category: Brzezinski K]] | |||
[[Category: Gawel M]] | |||
[[Category: Malecki PH]] | |||
Latest revision as of 14:51, 30 October 2024
Crystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ionsCrystal structure of Pseudomonas aeruginosa S-adenosyl-L-homocysteine hydrolase soaked with Cu+ ions
Structural highlights
FunctionSAHH_PSEAE May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. Publication Abstract from PubMedWe report biochemical and structural studies on inhibiting bacterial S-adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor. A closer look at molecular mechanisms underlying inhibition of S-adenosyl-L-homocysteine hydrolase by transition metal cations.,Gawel M, Malecki PH, Sliwiak J, Stepniewska M, Imiolczyk B, Czyrko-Horczak J, Jakubczyk D, Marczak L, Plonska-Brzezinska ME, Brzezinski K Chem Commun (Camb). 2024 Oct 8;60(81):11504-11507. doi: 10.1039/d4cc03143a. PMID:39230573[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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