3tms: Difference between revisions

Revision as of 13:09, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3tms.png

Template:STRUCTURE 3tms

PLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASESPLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASES

Template:ABSTRACT PUBMED 2128651

About this StructureAbout this Structure

3TMS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases., Perry KM, Fauman EB, Finer-Moore JS, Montfort WR, Maley GF, Maley F, Stroud RM, Proteins. 1990;8(4):315-33. PMID:2128651

Page seeded by OCA on Thu Jul 3 13:09:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3tms.jpg|left|200px]]
+{{Seed}}
+[[Image:3tms.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3tms|  PDB=3tms  |  SCENE=  }}
-'''PLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASES'''
+===PLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASES===
-==Overview==
+<!--
-The structure of thymidylate synthase (TS) from Escherichia coli was solved from cubic crystals with a = 133 A grown under reducing conditions at pH 7.0, and refined to R = 22% at 2.1 A resolution. The structure is compared with that from Lactobacillus casei solved to R = 21% at 2.3 A resolution. The structures are compared using a difference distance matrix, which identifies a common core of residues that retains the same relationship to one another in both species. After subtraction of the effects of a 50 amino acid insert present in Lactobacillus casei, differences in position of atoms correlate with temperature factors and with distance from the nearest substituted residue. The dependence of structural difference on thermal factor is parameterized and reflects both errors in coordinates that correlate with thermal factor, and the increased width of the energy well in which atoms of high thermal factor lie. The dependence of structural difference on distance from the nearest substitution also depends on thermal factors and shows an exponential dependence with half maximal effect at 3.0 A from the substitution. This represents the plastic accommodation of the protein which is parameterized in terms of thermal B factor and distance from a mutational change.
+The line below this paragraph, {{ABSTRACT_PUBMED_2128651}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2128651 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_2128651}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Perry, K M.]]
 [[Category: Stroud, R M.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:14:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:09:51 2008''