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2k7j

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Revision as of 10:34, 18 July 2018

Human Acylphosphatase(AcPh) surface charge-optimized

Structural highlights

2k7j is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2k7k
Gene:	ACYP1, ACYPE (HUMAN)
Activity:	Acylphosphatase, with EC number 3.6.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACYP1_HUMAN] Its physiological role is not yet clear.

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

Here, we report the application of a computational approach that allows the rational design of enzymes with enhanced thermostability while retaining full enzymatic activity. The approach is based on the optimization of the energy of charge-charge interactions on the protein surface. We experimentally tested the validity of the approach on 2 human enzymes, acylphosphatase (AcPh) and Cdc42 GTPase, that differ in size (98 vs. 198-aa residues, respectively) and tertiary structure. We show that the designed proteins are significantly more stable than the corresponding WT proteins. The increase in stability is not accompanied by significant changes in structure, oligomerization state, or, most importantly, activity of the designed AcPh or Cdc42. This success of the design methodology suggests that it can be universally applied to other enzymes, on its own or in combination with the other strategies based on redesign of the interactions in the protein core.

Rational stabilization of enzymes by computational redesign of surface charge-charge interactions.,Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI Proc Natl Acad Sci U S A. 2009 Feb 5. PMID:19196981^[1]

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

References

↑ Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI. Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Proc Natl Acad Sci U S A. 2009 Feb 5. PMID:19196981

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k7j"

@@ Line 1: / Line 1: @@
 ==Human Acylphosphatase(AcPh) surface charge-optimized==
 <StructureSection load='2k7j' size='340' side='right' caption='[[2k7j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACYP1, ACYPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylphosphatase Acylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.7 3.6.1.7] </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=2k7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7j OCA], [http://pdbe.org/2k7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k7j RCSB], [http://www.ebi.ac.uk/pdbsum/2k7j 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=2k7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7j OCA], [http://pdbe.org/2k7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k7j RCSB], [http://www.ebi.ac.uk/pdbsum/2k7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7j_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7j_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 41: / Line 42: @@
 [[Category: Patel, M M]]
 [[Category: Wang, C]]
+[[Category: Acetylation]]
 [[Category: Hydrolase]]
 [[Category: Protein]]

2k7j

From Proteopedia

Revision as of 10:34, 18 July 2018

Human Acylphosphatase(AcPh) surface charge-optimized

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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