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1l23

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Revision as of 06:41, 29 November 2017

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING

Structural highlights

1l23 is a 1 chain structure with sequence from Bpt4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2lzm, 1l01, 1l02, 1l03, 1l04, 1l05, 1l06, 1l07, 1l08, 1l09, 1l10, 1l11, 1l12, 1l13, 1l14, 1l15, 1l16, 1l17, 1l18, 1l19, 1l20, 1l21, 1l22, 1l24, 1l25, 1l26, 1l27, 1l28, 1l29, 1l30, 1l31, 1l32, 1l33, 1l34, 1l35, 1l36
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYS_BPT4] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.

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

It is proposed that the stability of a protein can be increased by selected amino acid substitutions that decrease the configurational entropy of unfolding. Two such substitutions, one of the form Xaa----Pro and the other of the form Gly----Xaa, were constructed in bacteriophage T4 lysozyme at sites consistent with the known three-dimensional structure. Both substitutions stabilize the protein toward reversible and irreversible thermal denaturation at physiological pH. The substitutions have no effect on enzymatic activity. High-resolution crystallographic analysis of the proline-containing mutant protein (Ala-82----Pro) shows that its three-dimensional structure is essentially identical with the wild-type enzyme. The overall structure of the other mutant enzyme (Gly-77----Ala) is also very similar to wild-type lysozyme, although there are localized conformational adjustments in the vicinity of the altered amino acid. The combination of a number of such amino acid replacements, each of which is expected to contribute approximately 1 kcal/mol (1 cal = 4.184 J) to the free energy of folding, may provide a general strategy for substantial improvement in the stability of a protein.

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.,Matthews BW, Nicholson H, Becktel WJ Proc Natl Acad Sci U S A. 1987 Oct;84(19):6663-7. PMID:3477797^[1]

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

References

↑ Matthews BW, Nicholson H, Becktel WJ. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6663-7. PMID:3477797

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/1l23"

Categories: Bpt4 | Lysozyme | Matthews, B W | Nicholson, H

@@ Line 1: / Line 1: @@
 ==ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING==
 <StructureSection load='1l23' size='340' side='right' caption='[[1l23]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lzm|2lzm]], [[1l01|1l01]], [[1l02|1l02]], [[1l03|1l03]], [[1l04|1l04]], [[1l05|1l05]], [[1l06|1l06]], [[1l07|1l07]], [[1l08|1l08]], [[1l09|1l09]], [[1l10|1l10]], [[1l11|1l11]], [[1l12|1l12]], [[1l13|1l13]], [[1l14|1l14]], [[1l15|1l15]], [[1l16|1l16]], [[1l17|1l17]], [[1l18|1l18]], [[1l19|1l19]], [[1l20|1l20]], [[1l21|1l21]], [[1l22|1l22]], [[1l24|1l24]], [[1l25|1l25]], [[1l26|1l26]], [[1l27|1l27]], [[1l28|1l28]], [[1l29|1l29]], [[1l30|1l30]], [[1l31|1l31]], [[1l32|1l32]], [[1l33|1l33]], [[1l34|1l34]], [[1l35|1l35]], [[1l36|1l36]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=1l23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l23 OCA], [http://pdbe.org/1l23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l23 RCSB], [http://www.ebi.ac.uk/pdbsum/1l23 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=1l23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l23 OCA], [http://pdbe.org/1l23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l23 RCSB], [http://www.ebi.ac.uk/pdbsum/1l23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l23 ProSAT]</span></td></tr>
 </table>
 == Function ==

1l23

From Proteopedia

Revision as of 06:41, 29 November 2017

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING

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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