1c3c: Difference between revisions

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[[Image:1c3c.gif|left|200px]]


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==T. MARITIMA ADENYLOSUCCINATE LYASE==
The line below this paragraph, containing "STRUCTURE_1c3c", creates the "Structure Box" on the page.
<StructureSection load='1c3c' size='340' side='right'caption='[[1c3c]], [[Resolution|resolution]] 1.80&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'>[[1c3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C3C 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]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3c OCA], [https://pdbe.org/1c3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c3c RCSB], [https://www.ebi.ac.uk/pdbsum/1c3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c3c ProSAT]</span></td></tr>
{{STRUCTURE_1c3c|  PDB=1c3c |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/PUR8_THEMA PUR8_THEMA]
== 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/c3/1c3c_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=1c3c ConSurf].
<div style="clear:both"></div>


'''T. MARITIMA ADENYLOSUCCINATE LYASE'''
==See Also==
 
*[[Adenylosuccinate lyase 3D structures|Adenylosuccinate lyase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Background: Adenylosuccinate lyase is an enzyme that plays a critical role in both cellular replication and metabolism via its action in the de novo purine biosynthetic pathway. Adenylosuccinate lyase is the only enzyme in this pathway to catalyze two separate reactions, enabling it to participate in the addition of a nitrogen at two different positions in adenosine monophosphate. Both reactions catalyzed by adenylosuccinate lyase involve the beta-elimination of fumarate. Enzymes that catalyze this type of reaction belong to a superfamily, the members of which are homotetramers. Because adenylosuccinate lyase plays an integral part in maintaining proper cellular metabolism, mutations in the human enzyme can have severe clinical consequences, including mental retardation with autistic features. Results: The 1.8 A crystal structure of adenylosuccinate lyase from Thermotoga maritima has been determined by multiwavelength anomalous dispersion using the selenomethionine-substituted enzyme. The fold of the monomer is reminiscent of other members of the beta-elimination superfamily. However, its active tetrameric form exhibits striking differences in active-site architecture and cleft size. Conclusions: This first structure of an adenylosuccinate lyase reveals that, along with the catalytic base (His141) and the catalytic acid (His68), Gln212 and Asn270 might play a vital role in catalysis by properly orienting the succinyl moiety of the substrates. We propose a model for the dual activity of adenylosuccinate lyase: a single 180 degrees bond rotation must occur in the substrate between the first and second enzymatic reactions. Modeling of the pathogenic human S413P mutation indicates that the mutation destabilizes the enzyme by disrupting the C-terminal extension.
[[Category: Large Structures]]
 
==About this Structure==
1C3C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3C OCA].
 
==Reference==
The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway., Toth EA, Yeates TO, Structure. 2000 Feb 15;8(2):163-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10673438 10673438]
[[Category: Adenylosuccinate lyase]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Toth, E A.]]
[[Category: Toth EA]]
[[Category: Yeates, T O.]]
[[Category: Yeates TO]]
[[Category: Lyase]]
[[Category: Purine biosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:16:40 2008''

Latest revision as of 09:40, 7 February 2024

T. MARITIMA ADENYLOSUCCINATE LYASET. MARITIMA ADENYLOSUCCINATE LYASE

Structural highlights

1c3c is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PUR8_THEMA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1c3c, resolution 1.80Å

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