2fl1: Difference between revisions

Revision as of 13:04, 28 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:2fl1.png

Template:STRUCTURE 2fl1

Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolutionCrystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution

Template:ABSTRACT PUBMED 16627946

About this StructureAbout this Structure

2FL1 is a Single protein structure of sequence from Zoanthus sp.. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a red fluorescent protein from Zoanthus, zRFP574, reveals a novel chromophore., Pletneva N, Pletnev S, Tikhonova T, Popov V, Martynov V, Pletnev V, Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):527-32. Epub 2006, Apr 19. PMID:16627946

Page seeded by OCA on Mon Jul 28 13:04:08 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2fl1.jpg|left|200px]]
+{{Seed}}
+[[Image:2fl1.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2fl1|  PDB=2fl1  |  SCENE=  }}
-'''Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution'''
+===Crystal structure of red fluorescent protein from Zoanthus, zRFP574, at 2.4A resolution===
-==Overview==
+<!--
-The three-dimensional structure of the red fluorescent protein (RFP) zRFP574 from the button polyp Zoanthus sp. (two dimers per asymmetric unit, 231 x 4 amino acids) has been determined at 2.4 A resolution in space group C222(1). The crystal structure, refined to a crystallographic R factor of 0.203 (R(free) = 0.249), adopts the beta-barrel fold composed of 11 strands similar to that of the yellow fluorescent protein zYFP538. The zRFP574 chromophore, originating from the protein sequence Asp66-Tyr67-Gly68, has a two-ring structure typical of GFP-like proteins. The bond geometry of residue 66 shows the strong tendency of the corresponding C(alpha) atom to sp(2) hybridization as a consequence of N-acylimine bond formation. The zRFP574 chromophore contains the 65-66 cis-peptide bond characteristic of red fluorescent proteins. The chromophore phenolic ring adopts a cis conformation coplanar with the imidazolinone ring. The crystallographic study has revealed an unexpected chemical feature of the internal chromophore. A decarboxylated side chain of the chromophore-forming residue Asp66 has been observed in the structure. This additional post-translational modification is likely to play a key role in the bathochromic shift of the zRFP574 spectrum.
+The line below this paragraph, {{ABSTRACT_PUBMED_16627946}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16627946 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16627946}}
 ==About this Structure==
@@ Line 40: / Line 44: @@
 [[Category: Zoanthus sp.]]
 [[Category: Zrfp574]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:00:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:04:08 2008''