2gaw: Difference between revisions

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New page: left|200px<br /> <applet load="2gaw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gaw, resolution 2.2Å" /> '''WILD TYPE GLYCOSYLAS...
 
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[[Image:2gaw.gif|left|200px]]<br />
<applet load="2gaw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2gaw, resolution 2.2&Aring;" />
'''WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM'''<br />


==Overview==
==WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM==
Glycosylasparaginase (GA) is a member of a novel family of N-terminal, nucleophile hydrolases that catalytically use an N-terminal residue as, both a polarizing base and a nucleophile. These enzymes are activated from, a single chain precursor by intramolecular autoproteolysis to yield the, N-terminal nucleophile. A deficiency of GA results in the human genetic, disorder known as aspartylglycosaminuria. In this study, we report the, crystal structure of recombinant GA from Flavobacterium meningosepticum., Similar to the human structure, the bacterial GA forms an, alphabetabetaalpha sandwich. However, some significant differences are, observed between the Flavobacterium and human structures. The active site, of Flavobacterium glycosylasparaginase is in an open conformation when, compared ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9685368 (full description)]]
<StructureSection load='2gaw' size='340' side='right'caption='[[2gaw]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gaw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GAW 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]] 2.2&#8491;</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=2gaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gaw OCA], [https://pdbe.org/2gaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gaw RCSB], [https://www.ebi.ac.uk/pdbsum/2gaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gaw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASPG_ELIMR ASPG_ELIMR] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.
== 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/ga/2gaw_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=2gaw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2GAW is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Flavobacterium_meningosepticum Flavobacterium meningosepticum]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GAW OCA]].
*[[Glycosylasparaginase|Glycosylasparaginase]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis., Guo HC, Xu Q, Buckley D, Guan C, J Biol Chem. 1998 Aug 7;273(32):20205-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9685368 9685368]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Flavobacterium meningosepticum]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Guo H-C]]
[[Category: Guo, H.C.]]
[[Category: Xu Q]]
[[Category: Xu, Q.]]
[[Category: autoproteolysis]]
[[Category: glycosylasparaginase]]
[[Category: n-terminal nucleophile hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:13:39 2007''

Latest revision as of 12:26, 14 February 2024

WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUMWILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

Structural highlights

2gaw is a 4 chain structure with sequence from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASPG_ELIMR Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.

Evolutionary Conservation

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

See Also

2gaw, resolution 2.20Å

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