137l

From Proteopedia

(Difference between revisions)

Revision as of 10:24, 14 July 2021

STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY

Structural highlights

137l is a 2 chain structure with sequence from Bpt4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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

The propensity of an amino acid to form an alpha helix in a protein was determined by multiple amino substitutions at positions 44 and 131 in T4 lysozyme. These positions are solvent-exposed sites within the alpha helices that comprise, respectively, residues 39 to 50 and 126 to 134. Except for two acidic substitutions that may be involved in salt bridges, the changes in stability at the two sites agree well. The stability values also agree with those observed for corresponding amino acid substitutions in some model peptides. Thus, helix propensity values derived from model peptides can be applicable to proteins. Among the 20 naturally occurring amino acids, proline, glycine, and alanine each have a structurally unique feature that helps to explain their low or high helix propensities. For the remaining 17 amino acids, it appears that the side chain hydrophobic surface buried against the side of the helix contributes substantially to alpha helix propensity.

Structural basis of amino acid alpha helix propensity.,Blaber M, Zhang XJ, Matthews BW Science. 1993 Jun 11;260(5114):1637-40. PMID:8503008^[1]

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

References

↑ Blaber M, Zhang XJ, Matthews BW. Structural basis of amino acid alpha helix propensity. Science. 1993 Jun 11;260(5114):1637-40. PMID:8503008

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/137l"

Categories: Bpt4 | Large Structures | Lysozyme | Blaber, M | Matthews, B W

@@ Line 3: / Line 3: @@
 <StructureSection load='137l' size='340' side='right'caption='[[137l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[137l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=137L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=137L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[137l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=137L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=137L 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/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>
+</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://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=137l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=137l OCA], [http://pdbe.org/137l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=137l RCSB], [http://www.ebi.ac.uk/pdbsum/137l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=137l ProSAT]</span></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=137l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=137l OCA], [https://pdbe.org/137l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=137l RCSB], [https://www.ebi.ac.uk/pdbsum/137l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=137l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
+[[https://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

137l

From Proteopedia

Revision as of 10:24, 14 July 2021

STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY

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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