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[[Image:1mf1.jpg|left|200px]]


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==Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with AMP==
The line below this paragraph, containing "STRUCTURE_1mf1", creates the "Structure Box" on the page.
<StructureSection load='1mf1' size='340' side='right'caption='[[1mf1]], [[Resolution|resolution]] 2.70&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'>[[1mf1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MF1 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]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
{{STRUCTURE_1mf1| PDB=1mf1 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mf1 OCA], [https://pdbe.org/1mf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mf1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PURA1_MOUSE PURA1_MOUSE] Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.<ref>PMID:12482871</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/mf/1mf1_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=1mf1 ConSurf].
<div style="clear:both"></div>


'''Structure of the Recombinant Mouse-Muscle Adenylosuccinate Synthetase Complexed with AMP'''
==See Also==
 
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
 
== References ==
==Overview==
<references/>
Adenylosuccinate synthetase governs the committed step of AMP biosynthesis, the generation of 6-phosphoryl-IMP from GTP and IMP followed by the formation of adenylosuccinate from 6-phosphoryl-IMP and l-aspartate. The enzyme is subject to feedback inhibition by AMP and adenylosuccinate, but crystallographic complexes of the mouse muscle synthetase presented here infer mechanisms of inhibition that involve potentially synergistic ligand combinations. AMP alone adopts the productive binding mode of IMP and yet stabilizes the active site in a conformation that favors the binding of Mg(2+)-IMP to the GTP pocket. On the other hand, AMP, in the presence of GDP, orthophosphate, and Mg(2+), adopts the binding mode of adenylosuccinate. Depending on circumstances then, AMP behaves as an analogue of IMP or as an analogue of adenylosuccinate. The complex of adenylosuccinate.GDP.Mg(2+).sulfate, the first structure of an adenylosuccinate-bound synthetase, reveals significant geometric distortions and tight nonbonded contacts relevant to the proposed catalytic mechanism. Adenylosuccinate forms from 6-phosphoryl-IMP and l-aspartate by the movement of the purine ring into the alpha-amino group of l-aspartate.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1MF1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MF1 OCA].
 
==Reference==
Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase., Iancu CV, Borza T, Fromm HJ, Honzatko RB, J Biol Chem. 2002 Oct 25;277(43):40536-43. Epub 2002 Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12186864 12186864]
[[Category: Adenylosuccinate synthase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Borza T]]
[[Category: Borza, T.]]
[[Category: Fromm HJ]]
[[Category: Fromm, H J.]]
[[Category: Honzatko RB]]
[[Category: Honzatko, R B.]]
[[Category: Iancu CV]]
[[Category: Iancu, C V.]]
[[Category: Gtp-binding]]
[[Category: Multigene family]]
[[Category: Purine biosynthesis]]
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