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.


5ghq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:12, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of human MTH1(G2K/D120A mutant) in complex with 2-oxo-dATP under high concentrations of 2-oxo-dATP==
==Crystal structure of human MTH1(G2K/D120A mutant) in complex with 2-oxo-dATP under high concentrations of 2-oxo-dATP==
-
<StructureSection load='5ghq' size='340' side='right' caption='[[5ghq]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
+
<StructureSection load='5ghq' size='340' side='right'caption='[[5ghq]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5ghq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GHQ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5ghq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GHQ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6U4:[[(2R,3S,5R)-5-(6-AZANYL-2-OXIDANYLIDENE-1H-PURIN-9-YL)-3-OXIDANYL-OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+PHOSPHONO+HYDROGEN+PHOSPHATE'>6U4</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.181&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ghi|5ghi]], [[5ghj|5ghj]], [[5ghm|5ghm]], [[5ghn|5ghn]], [[5gho|5gho]], [[5ghp|5ghp]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6U4:[[(2R,3S,5R)-5-(6-AZANYL-2-OXIDANYLIDENE-1H-PURIN-9-YL)-3-OXIDANYL-OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+PHOSPHONO+HYDROGEN+PHOSPHATE'>6U4</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5ghq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghq OCA], [http://pdbe.org/5ghq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ghq RCSB], [http://www.ebi.ac.uk/pdbsum/5ghq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghq 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=5ghq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghq OCA], [https://pdbe.org/5ghq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ghq RCSB], [https://www.ebi.ac.uk/pdbsum/5ghq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/8ODP_HUMAN 8ODP_HUMAN]] Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP.<ref>PMID:10373420</ref> <ref>PMID:10608900</ref> <ref>PMID:11139615</ref> <ref>PMID:12857738</ref> <ref>PMID:22556419</ref>
+
[https://www.uniprot.org/uniprot/8ODP_HUMAN 8ODP_HUMAN] Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP.<ref>PMID:10373420</ref> <ref>PMID:10608900</ref> <ref>PMID:11139615</ref> <ref>PMID:12857738</ref> <ref>PMID:22556419</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Human MTH1 (hMTH1) is an enzyme that hydrolyses several oxidized purine nucleoside triphosphates to their corresponding nucleoside monophosphates. Crystallographic studies have shown that the accurate mode of interaction between 8-oxoguanine and hMTH1 cannot be understood without determining the positions of the H atoms, as can be observed in neutron and/or ultrahigh-resolution X-ray diffraction studies. The hMTH1 protein prepared in the original expression system from Escherichia coli did not appear to be suitable for obtaining high-quality crystals because the hMTH1 protein had heterogeneous N-termini of Met1 and Gly2 that resulted from N-terminal Met excision by methionine aminopeptidase from the E. coli host. To obtain homogeneous hMTH1, the Gly at the second position was replaced by Lys. As a result, mutant hMTH1 protein [hMTH1(G2K)] with a homogeneous N-terminus could be prepared and high-quality crystals which diffracted to near 1.1 A resolution using synchrotron radiation were produced. The new crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.36, b = 47.58, c = 123.89 A.
+
-
Crystallization and preliminary X-ray analysis of human MTH1 with a homogeneous N-terminus.,Koga Y, Inazato M, Nakamura T, Hashikawa C, Chirifu M, Michi A, Yamashita T, Toma S, Kuniyasu A, Ikemizu S, Nakabeppu Y, Yamagata Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):45-8. doi: , 10.1107/S1744309112048002. Epub 2012 Dec 20. PMID:23295485<ref>PMID:23295485</ref>
+
==See Also==
-
 
+
*[[7%2C8-dihydro-8-oxoguanine triphosphatase 3D structures|7%2C8-dihydro-8-oxoguanine triphosphatase 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5ghq" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Hirata, K]]
+
[[Category: Homo sapiens]]
-
[[Category: Nakabeppu, Y]]
+
[[Category: Large Structures]]
-
[[Category: Nakamura, T]]
+
[[Category: Hirata K]]
-
[[Category: Waz, S]]
+
[[Category: Nakabeppu Y]]
-
[[Category: Yamagata, Y]]
+
[[Category: Nakamura T]]
-
[[Category: Alpha-beta-alpha sandwich]]
+
[[Category: Waz S]]
-
[[Category: Dna damage]]
+
[[Category: Yamagata Y]]
-
[[Category: Dna repair]]
+
-
[[Category: Dna replication]]
+
-
[[Category: Hydrolase]]
+

Current revision

Crystal structure of human MTH1(G2K/D120A mutant) in complex with 2-oxo-dATP under high concentrations of 2-oxo-dATP

PDB ID 5ghq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools