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.


2hji

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:02, 29 May 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2hji.png|left|200px]]
 
-
<!--
+
==Structural model for the Fe-containing isoform of acireductone dioxygenase==
-
The line below this paragraph, containing "STRUCTURE_2hji", creates the "Structure Box" on the page.
+
<StructureSection load='2hji' size='340' side='right'caption='[[2hji]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2hji]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HJI FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-
{{STRUCTURE_2hji| PDB=2hji | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hji OCA], [https://pdbe.org/2hji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hji RCSB], [https://www.ebi.ac.uk/pdbsum/2hji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hji ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MTND_KLEOX MTND_KLEOX] Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.<ref>PMID:8407993</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/2hji_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=2hji ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni2+ -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe2+ is bound (ARD'), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe2+ renders the active site of ARD' inaccessible to standard NMR methods. The structure of ARD' has been determined using Fe2+ binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD'. ARD' retains the beta-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the beta-sandwich and decreases order at the other upon interconversion of ARD and ARD', causing loss of the C-terminal helix in ARD' and rearrangements of residues involved in substrate orientation in the active site.
-
===Structural model for the Fe-containing isoform of acireductone dioxygenase===
+
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase.,Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC J Mol Biol. 2006 Nov 3;363(4):823-34. Epub 2006 Aug 26. PMID:16989860<ref>PMID:16989860</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_16989860}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2hji" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 16989860 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16989860}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2HJI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJI OCA].
+
-
 
+
-
==Reference==
+
-
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase., Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC, J Mol Biol. 2006 Nov 3;363(4):823-34. Epub 2006 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16989860 16989860]
+
-
 
+
-
One protein, two enzymes., Dai Y, Wensink PC, Abeles RH, J Biol Chem. 1999 Jan 15;274(3):1193-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9880484 9880484]
+
[[Category: Klebsiella oxytoca]]
[[Category: Klebsiella oxytoca]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Chai, S C.]]
+
[[Category: Chai SC]]
-
[[Category: Ju, T.]]
+
[[Category: Ju T]]
-
[[Category: Maroney, M J.]]
+
[[Category: Maroney MJ]]
-
[[Category: Pochapsky, T C.]]
+
[[Category: Pochapsky TC]]
-
[[Category: Dioxygenase]]
+
-
[[Category: Isozyme]]
+
-
[[Category: Methionine salvage]]
+
-
[[Category: Non-heme iron]]
+
-
[[Category: Structural entropy]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:05:35 2008''
+

Current revision

Structural model for the Fe-containing isoform of acireductone dioxygenase

PDB ID 2hji

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/2hji"
Personal tools