This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kwg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:26, 13 March 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1kwg.gif|left|200px]]<br /><applet load="1kwg" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1kwg, resolution 1.60&Aring;" />
 
-
'''Crystal structure of Thermus thermophilus A4 beta-galactosidase'''<br />
 
-
==Overview==
+
==Crystal structure of Thermus thermophilus A4 beta-galactosidase==
-
The beta-galactosidase from an extreme thermophile, Thermus thermophilus A4 (A4-beta-Gal), is thermostable and belongs to the glycoside hydrolase family 42 (GH-42). As the first known structures of a GH-42 enzyme, we determined the crystal structures of free and galactose-bound A4-beta-Gal at 1.6A and 2.2A resolution, respectively. A4-beta-Gal forms a homotrimeric structure resembling a flowerpot. Each monomer has an active site located inside a large central tunnel. The N-terminal domain of A4-beta-Gal has a TIM barrel fold, as predicted from hydrophobic cluster analysis. The putative catalytic residues of A4-beta-Gal (Glu141 and Glu312) superimpose well with the catalytic residues of Escherichia coli beta-galactosidase. The environment around the catalytic nucleophile (Glu312) is similar to that in the case of E.coli beta-galactosidase, but the recognition mechanism for a substrate is different. Trp182 of the next subunit of the trimer constitutes a part of the active-site pocket, indicating that the trimeric structure is essential for the enzyme activity. Structural comparison with other glycoside hydrolases revealed that many features of the 4/7 superfamily are conserved in the A4-beta-Gal structure. On the basis of the results of 1H NMR spectroscopy, A4-beta-Gal was determined to be a "retaining" enzyme. Interestingly, the active site was similar with those of retaining enzymes, but the overall fold of the TIM barrel domain was very similar to that of an inverting enzyme, beta-amylase.
+
<StructureSection load='1kwg' size='340' side='right'caption='[[1kwg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1kwg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KWG 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]] 1.6&#8491;</td></tr>
 +
<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1kwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwg OCA], [https://pdbe.org/1kwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kwg RCSB], [https://www.ebi.ac.uk/pdbsum/1kwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwg ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/BGAL_THETH BGAL_THETH]
 +
== 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/kw/1kwg_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=1kwg ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1KWG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWG OCA].
+
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose., Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T, J Mol Biol. 2002 Sep 6;322(1):79-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12215416 12215416]
+
[[Category: Large Structures]]
-
[[Category: Beta-galactosidase]]
+
-
[[Category: Single protein]]
+
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
-
[[Category: Fushinobu, S.]]
+
[[Category: Fushinobu S]]
-
[[Category: Hidaka, M.]]
+
[[Category: Hidaka M]]
-
[[Category: Matsuzawa, H.]]
+
[[Category: Matsuzawa H]]
-
[[Category: Motoshima, H.]]
+
[[Category: Motoshima H]]
-
[[Category: Ohtsu, N.]]
+
[[Category: Ohtsu N]]
-
[[Category: Shoun, H.]]
+
[[Category: Shoun H]]
-
[[Category: Wakagi, T.]]
+
[[Category: Wakagi T]]
-
[[Category: ACT]]
+
-
[[Category: CL]]
+
-
[[Category: MPD]]
+
-
[[Category: ZN]]
+
-
[[Category: glycoside hydrolase family 42]]
+
-
[[Category: tim barrel]]
+
-
[[Category: trimer]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:43 2008''
+

Current revision

Crystal structure of Thermus thermophilus A4 beta-galactosidase

PDB ID 1kwg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools