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.


3hpa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:01, 21 February 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of an amidohydrolase gi:44264246 from an evironmental sample of sargasso sea==
==Crystal structure of an amidohydrolase gi:44264246 from an evironmental sample of sargasso sea==
-
<StructureSection load='3hpa' size='340' side='right' caption='[[3hpa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+
<StructureSection load='3hpa' size='340' side='right'caption='[[3hpa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3hpa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h4u 3h4u]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HPA FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3hpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h4u 3h4u]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HPA FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h4u|3h4u]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3hpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hpa OCA], [http://pdbe.org/3hpa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hpa RCSB], [http://www.ebi.ac.uk/pdbsum/3hpa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hpa 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=3hpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hpa OCA], [https://pdbe.org/3hpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hpa RCSB], [https://www.ebi.ac.uk/pdbsum/3hpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hpa ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
Line 18: Line 18:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hpa ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hpa ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
An enzyme from Pseudomonas aeruginosa, Pa0142 (gi|9945972), that is able to catalyze the deamination of 8-oxoguanine (8-oxoG) to uric acid has been identified for the first time. 8-Oxoguanine is formed by the oxidation of guanine residues within DNA by reactive oxygen species, and this lesion results in G:C to T:A transversions. The value of k(cat)/K(m) for the deamination of 8-oxoG by Pa0142 at pH 8.0 and 30 degrees C is 2.0 x 10(4) M(-1) s(-1). This enzyme can also catalyze the deamination of isocystosine and guanine at rates that are approximately an order of magnitude lower. The three-dimensional structure of a homologous enzyme (gi|44264246) from the Sargasso Sea has been determined by X-ray diffraction methods to a resolution of 2.2 A (PDB entry). The enzyme folds as a (beta/alpha)(8) barrel and is a member of the amidohydrolase superfamily with a single zinc in the active site. This enzyme catalyzes the deamination of 8-oxoG with a k(cat)/K(m) value of 2.7 x 10(5) M(-1) s(-1). Computational docking of potential high-energy intermediates for the deamination reaction to the X-ray crystal structure suggests that active-site binding of 8-oxoG is facilitated by hydrogen-bond interactions from a conserved glutamine that follows beta-strand 1 with the carbonyl group at C6, a conserved tyrosine that follows beta-strand 2 with N7, and a conserved cysteine residue that follows beta-strand 4 with the carbonyl group at C8. A bioinformatic analysis of available protein sequences suggests that approximately 200 other bacteria possess an enzyme capable of catalyzing the deamination of 8-oxoG.
 
- 
-
The hunt for 8-oxoguanine deaminase.,Hall RS, Fedorov AA, Marti-Arbona R, Fedorov EV, Kolb P, Sauder JM, Burley SK, Shoichet BK, Almo SC, Raushel FM J Am Chem Soc. 2010 Feb 17;132(6):1762-3. PMID:20088583<ref>PMID:20088583</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 3hpa" style="background-color:#fffaf0;"></div>
 
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Miscellaneous nucleic acid]]
+
[[Category: Large Structures]]
-
[[Category: Almo, S C]]
+
[[Category: Unidentified]]
-
[[Category: Burley, S K]]
+
[[Category: Almo SC]]
-
[[Category: Fedorov, A A]]
+
[[Category: Burley SK]]
-
[[Category: Fedorov, E V]]
+
[[Category: Fedorov AA]]
-
[[Category: Structural genomic]]
+
[[Category: Fedorov EV]]
-
[[Category: Raushel, F M]]
+
[[Category: Raushel FM]]
-
[[Category: Toro, R]]
+
[[Category: Toro R]]
-
[[Category: Amidohydrolase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
+
-
[[Category: PSI, Protein structure initiative]]
+
-
[[Category: Signature of zn ligand]]
+
-
[[Category: Target 9236e]]
+

Current revision

Crystal structure of an amidohydrolase gi:44264246 from an evironmental sample of sargasso sea

PDB ID 3hpa

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools