1qdl: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1qdl.jpg|left|200px]]<br /><applet load="1qdl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qdl, resolution 2.500&Aring;" />
'''THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS'''<br />


==Overview==
==THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS==
Anthranilate synthase catalyzes the synthesis of anthranilate from chorismate and glutamine and is feedback-inhibited by tryptophan. The enzyme of the hyperthermophile Sulfolobus solfataricus has been crystallized in the absence of physiological ligands, and its three-dimensional structure has been determined at 2.5-A resolution with x-ray crystallography. It is a heterotetramer of anthranilate synthase (TrpE) and glutamine amidotransferase (TrpG) subunits, in which two TrpG:TrpE protomers associate mainly via the TrpG subunits. The small TrpG subunit (195 residues) has the known "triad" glutamine amidotransferase fold. The large TrpE subunit (421 residues) has a novel fold. It displays a cleft between two domains, the tips of which contact the TrpG subunit across its active site. Clusters of catalytically essential residues are located inside the cleft, spatially separated from clustered residues involved in feedback inhibition. The structure suggests a model in which chorismate binding triggers a relative movement of the two domain tips of the TrpE subunit, activating the TrpG subunit and creating a channel for passage of ammonia toward the active site of the TrpE subunit. Tryptophan presumably blocks this rearrangement, thus stabilizing the inactive states of both subunits. The structure of the TrpE subunit is a likely prototype for the related enzymes 4-amino 4-deoxychorismate synthase and isochorismate synthase.
<StructureSection load='1qdl' size='340' side='right'caption='[[1qdl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1qdl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QDL FirstGlance]. <br>
1QDL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Active as [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDL OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=1qdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdl OCA], [https://pdbe.org/1qdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qdl RCSB], [https://www.ebi.ac.uk/pdbsum/1qdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qdl ProSAT]</span></td></tr>
==Reference==
</table>
The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications., Knochel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN, Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9479-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10449718 10449718]
== Function ==
[[Category: Anthranilate synthase]]
[https://www.uniprot.org/uniprot/TRPE_SACS2 TRPE_SACS2] Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.<ref>PMID:10449718</ref>
[[Category: Protein complex]]
== Evolutionary Conservation ==
[[Category: Sulfolobus solfataricus]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Bauerle, R.]]
Check<jmol>
[[Category: Gonzalez, A.]]
  <jmolCheckbox>
[[Category: Hester, G.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qdl_consurf.spt"</scriptWhenChecked>
[[Category: Ivens, A.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Jansonius, J N.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Kirschner, K.]]
  </jmolCheckbox>
[[Category: Knoechel, T.]]
</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=1qdl ConSurf].
[[Category: Wilmanns, M.]]
<div style="clear:both"></div>
[[Category: allosteric interaction]]
== References ==
[[Category: anthranilate synthase]]
<references/>
[[Category: glutamine amidotransferase]]
__TOC__
[[Category: tryptophan biosynthesis]]
</StructureSection>
 
[[Category: Large Structures]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:32 2008''
[[Category: Saccharolobus solfataricus]]
[[Category: Bauerle R]]
[[Category: Gonzalez A]]
[[Category: Hester G]]
[[Category: Ivens A]]
[[Category: Jansonius JN]]
[[Category: Kirschner K]]
[[Category: Knoechel T]]
[[Category: Wilmanns M]]

Latest revision as of 11:15, 14 February 2024

THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUSTHE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS

Structural highlights

1qdl is a 2 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRPE_SACS2 Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.[1]

Evolutionary Conservation

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

References

  1. Knochel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN. The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications. Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9479-84. PMID:10449718

1qdl, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA