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[[Image:1hg1.gif|left|200px]]<br />
<applet load="1hg1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hg1, resolution 1.80&Aring;" />
'''X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND D-ASPARTATE'''<br />


==Overview==
==X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and D-aspartate==
Bacterial L-asparaginases, enzymes that catalyze the hydrolysis of, L-asparagine to aspartic acid, have been used for over 30 years as, therapeutic agents in the treatment of acute childhood lymphoblastic, leukemia. Other substrates of asparaginases include L-glutamine, D-asparagine, and succinic acid monoamide. In this report, we present, high-resolution crystal structures of the complexes of Erwinia, chrysanthemi L-asparaginase (ErA) with the products of such reactions that, also can serve as substrates, namely L-glutamic acid (L-Glu), D-aspartic, acid (D-Asp), and succinic acid (Suc). Comparison of the four independent, active sites within each complex indicates unique and specific binding of, the ligand molecules; the mode of binding is also similar between, complexes. The lack of the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11341830 (full description)]]
<StructureSection load='1hg1' size='340' side='right'caption='[[1hg1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hg1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HG1 FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</scene></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=1hg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hg1 OCA], [https://pdbe.org/1hg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hg1 RCSB], [https://www.ebi.ac.uk/pdbsum/1hg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hg1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASPG_DICCH ASPG_DICCH]
== 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/hg/1hg1_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=1hg1 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HG1 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]] with DAS as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1]]. Structure known Active Sites: AS1, AS2, AS3, AS4, LI1, LI2, LI3 and LI4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HG1 OCA]].
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase., Aghaiypour K, Wlodawer A, Lubkowski J, Biochemistry. 2001 May 15;40(19):5655-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11341830 11341830]
[[Category: Dickeya chrysanthemi]]
[[Category: Erwinia chrysanthemi]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Kolyani KA]]
[[Category: Kolyani, K.A.]]
[[Category: Lubkowski J]]
[[Category: Lubkowski, J.]]
[[Category: Wlodawer A]]
[[Category: Wlodawer, A.]]
[[Category: DAS]]
[[Category: asparaginase]]
[[Category: complex]]
[[Category: d-aspartate]]
[[Category: hydrolase]]
[[Category: structure]]
[[Category: x-ray]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:29:32 2007''

Latest revision as of 14:31, 27 March 2024

X-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and D-aspartateX-ray structure of the complex between Erwinia chrysanthemi L-asparaginase and D-aspartate

Structural highlights

1hg1 is a 4 chain structure with sequence from Dickeya chrysanthemi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASPG_DICCH

Evolutionary Conservation

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

See Also

1hg1, resolution 1.80Å

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