1q2e: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1q2e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2e, resolution 1.75Å" /> '''CELLOBIOHYDROLASE CE...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1q2e.jpg|left|200px]]<br /><applet load="1q2e" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q2e, resolution 1.75&Aring;" />
'''CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE'''<br />


==Overview==
==CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE==
The exo-loop of Trichoderma reesei cellobiohydrolase Cel7A forms the roof, of the active site tunnel at the catalytic centre. Mutants were designed, to study the role of this loop in crystalline cellulose degradation. A, hydrogen bond to substrate made by a tyrosine at the tip of the loop was, removed by the Y247F mutation. The mobility of the loop was reduced by, introducing a new disulphide bridge in the mutant D241C/D249C. The tip of, the loop was deleted in mutant Delta(G245-Y252). No major structural, disturbances were observed in the mutant enzymes, nor was the, thermostability of the enzyme affected by the mutations.The Y247F mutation, caused a slight k(cat) reduction on 4-nitrophenyl lactoside, but only a, small effect on cellulose hydrolysis. Deletion of the tip of the loop, increased both k(cat) and K(M) and gave reduced product inhibition., Increased activity was observed on amorphous cellulose, while only half, the original activity remained on crystalline cellulose. Stabilisation of, the exo-loop by the disulphide bridge enhanced the activity on both, amorphous and crystalline cellulose. The ratio Glc(2)/(Glc(3)+Glc(1)), released from cellulose, which is indicative of processive action, was, highest with Tr Cel7A wild-type enzyme and smallest with the deletion, mutant on both substrates. Based on these data it seems that the exo-loop, of Tr Cel7A has evolved to facilitate processive crystalline cellulose, degradation, which does not require significant conformational changes of, this loop.
<StructureSection load='1q2e' size='340' side='right'caption='[[1q2e]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1q2e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2E 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</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=1q2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2e OCA], [https://pdbe.org/1q2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2e RCSB], [https://www.ebi.ac.uk/pdbsum/1q2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
== 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/q2/1q2e_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=1q2e ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1Q2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with NAG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q2E OCA].
*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
 
*[[Glucanase 3D structures|Glucanase 3D structures]]
==Reference==
__TOC__
Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D., von Ossowski I, Stahlberg J, Koivula A, Piens K, Becker D, Boer H, Harle R, Harris M, Divne C, Mahdi S, Zhao Y, Driguez H, Claeyssens M, Sinnott ML, Teeri TT, J Mol Biol. 2003 Oct 31;333(4):817-29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14568538 14568538]
</StructureSection>
[[Category: Cellulose 1,4-beta-cellobiosidase]]
[[Category: Large Structures]]
[[Category: Hypocrea jecorina]]
[[Category: Trichoderma reesei]]
[[Category: Single protein]]
[[Category: Harris M]]
[[Category: Harris, M.]]
[[Category: Jones TA]]
[[Category: Jones, T.A.]]
[[Category: Stahlberg J]]
[[Category: Stahlberg, J.]]
[[Category: CA]]
[[Category: NAG]]
[[Category: cellotetraose]]
[[Category: cellulase]]
[[Category: cellulose degradation]]
[[Category: glycoprotein]]
[[Category: glycosidase]]
[[Category: glycosylated protein]]
[[Category: hydrolase]]
[[Category: loop deletion]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:19:53 2007''

Latest revision as of 09:00, 17 April 2024

CELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSECELLOBIOHYDROLASE CEL7A WITH LOOP DELETION 245-252 AND BOUND NON-HYDROLYSABLE CELLOTETRAOSE

Structural highlights

1q2e is a 2 chain structure with sequence from Trichoderma reesei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUX1_HYPJE The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Evolutionary Conservation

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

See Also

1q2e, resolution 1.75Å

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
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1q2e&oldid=4129709"