1uux

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:59, 13 December 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1uux.png|left|200px]]
 
-
<!--
+
==Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism==
-
The line below this paragraph, containing "STRUCTURE_1uux", creates the "Structure Box" on the page.
+
<StructureSection load='1uux' size='340' side='right'caption='[[1uux]], [[Resolution|resolution]] 1.60&Aring;' 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'>[[1uux]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UUX 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">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MTE:PHOSPHONIC+ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER'>MTE</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene></td></tr>
-
{{STRUCTURE_1uux| PDB=1uux | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uux OCA], [https://pdbe.org/1uux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uux RCSB], [https://www.ebi.ac.uk/pdbsum/1uux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uux ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CNX1_ARATH CNX1_ARATH] Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.<ref>PMID:15504727</ref> <ref>PMID:16636046</ref> <ref>PMID:12590921</ref> <ref>PMID:15306815</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/uu/1uux_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=1uux ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The molybdenum cofactor is part of the active site of all molybdenum-dependent enzymes, except nitrogenase. The molybdenum cofactor consists of molybdopterin, a phosphorylated pyranopterin, with an ene-dithiolate coordinating molybdenum. The same pyranopterin-based cofactor is involved in metal coordination of the homologous tungsten-containing enzymes found in archea. The molybdenum cofactor is synthesized by a highly conserved biosynthetic pathway. In plants, the multidomain protein Cnx1 catalyses the insertion of molybdenum into molybdopterin. The Cnx1 G domain (Cnx1G), whose crystal structure has been determined in its apo form, binds molybdopterin with high affinity and participates in the catalysis of molybdenum insertion. Here we present two high-resolution crystal structures of Cnx1G in complex with molybdopterin and with adenylated molybdopterin (molybdopterin-AMP), a mechanistically important intermediate. Molybdopterin-AMP is the reaction product of Cnx1G and is subsequently processed in a magnesium-dependent reaction by the amino-terminal E domain of Cnx1 to yield active molybdenum cofactor. The unexpected identification of copper bound to the molybdopterin dithiolate sulphurs in both structures, coupled with the observed copper inhibition of Cnx1G activity, provides a molecular link between molybdenum and copper metabolism.
-
===STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM===
+
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism.,Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G Nature. 2004 Aug 12;430(7001):803-6. PMID:15306815<ref>PMID:15306815</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_15306815}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1uux" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 15306815 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15306815}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1UUX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUX OCA].
+
-
 
+
-
==Reference==
+
-
Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism., Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G, Nature. 2004 Aug 12;430(7001):803-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15306815 15306815]
+
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Hecht, H J.]]
+
[[Category: Hecht HJ]]
-
[[Category: Kuper, J.]]
+
[[Category: Kuper J]]
-
[[Category: Llamas, A.]]
+
[[Category: Llamas A]]
-
[[Category: Mendel, R R.]]
+
[[Category: Mendel RR]]
-
[[Category: Schwarz, G.]]
+
[[Category: Schwarz G]]
-
[[Category: Chelatase]]
+
-
[[Category: Molybdenum cofactor biosynthesis]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:53:50 2008''
+

Current revision

Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism

PDB ID 1uux

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools