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1cud

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Revision as of 11:16, 24 August 2017

CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT

Structural highlights

1cud is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Triacylglycerol lipase, with EC number 3.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CUTI1_FUSSO] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection.

Evolutionary Conservation

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

Publication Abstract from PubMed

In characterizing mutants and covalently inhibited complexes of Fusarium solani cutinase, which is a 197-residue lipolytic enzyme, 34 variant structures, crystallizing in 8 different crystal forms, have been determined, mostly at high resolution. Taking advantage of this considerable body of information, a structural comparative analysis was carried out to investigate the dynamics of cutinase. Surface loops were identified as the major flexible protein regions, particularly those forming the active-site groove, whereas the elements constituting the protein scaffold were found to retain the same conformation in all the cutinase variants studied. Flexibility turned out to be correlated with thermal motion. With a given crystal packing environment, a high flexibility turned out to be correlated with a low involvement in crystal packing contacts. The high degree of crystal polymorphism, which allowed different conformations with similar energy to be detected, made it possible to identify motions which would have remained unidentified if only a single crystal form had been available. Fairly good agreement was found to exist between the data obtained from the structural comparison and those from a molecular dynamics (MD) simulation carried out on the native enzyme. The crystallographic approach used in this study turned out to be a suitable tool for investigating cutinase dynamics. Because of the availability of a set of closely related proteins in different crystal environments, the intrinsic drawback of a crystallographic approach was bypassed. By combining several static pictures, the dynamics of the protein could be monitored much more realistically than what can be achieved on the basis of static pictures alone.

Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants.,Longhi S, Nicolas A, Creveld L, Egmond M, Verrips CT, de Vlieg J, Martinez C, Cambillau C Proteins. 1996 Dec;26(4):442-58. PMID:8990497^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Longhi S, Nicolas A, Creveld L, Egmond M, Verrips CT, de Vlieg J, Martinez C, Cambillau C. Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Proteins. 1996 Dec;26(4):442-58. PMID:8990497 doi:<442::AID-PROT5>3.0.CO;2-D http://dx.doi.org/10.1002/(SICI)1097-0134(199612)26:4<442::AID-PROT5>3.0.CO;2-D

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cud"

@@ Line 1: / Line 1: @@
 ==CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT==
 <StructureSection load='1cud' size='340' side='right' caption='[[1cud]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cud]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Fusso Fusso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CUD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cud]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CUD FirstGlance]. <br>
 </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cud OCA], [http://pdbe.org/1cud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cud RCSB], [http://www.ebi.ac.uk/pdbsum/1cud PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cud OCA], [http://pdbe.org/1cud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cud RCSB], [http://www.ebi.ac.uk/pdbsum/1cud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cud ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1cud ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Fusso]]
 [[Category: Triacylglycerol lipase]]
 [[Category: Cambillau, C]]

1cud

From Proteopedia

Revision as of 11:16, 24 August 2017

CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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