1fpp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fpp.gif|left|200px]]<br /><applet load="1fpp" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1fpp.gif|left|200px]]
-
caption="1fpp, resolution 2.75&Aring;" />
+
 
-
'''PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE'''<br />
+
{{Structure
 +
|PDB= 1fpp |SIZE=350|CAPTION= <scene name='initialview01'>1fpp</scene>, resolution 2.75&Aring;
 +
|SITE= <scene name='pdbsite=ZN:Active-Site+Zn'>ZN</scene>
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FPP:FARNESYL DIPHOSPHATE'>FPP</scene>
 +
|ACTIVITY=
 +
|GENE= FNTA, FNTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
 +
}}
 +
 
 +
'''PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1FPP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=FPP:'>FPP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=ZN:Active-Site+Zn'>ZN</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPP OCA].
+
1FPP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPP OCA].
==Reference==
==Reference==
-
Protein farnesyltransferase: structure and implications for substrate binding., Dunten P, Kammlott U, Crowther R, Weber D, Palermo R, Birktoft J, Biochemistry. 1998 Jun 2;37(22):7907-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9609683 9609683]
+
Protein farnesyltransferase: structure and implications for substrate binding., Dunten P, Kammlott U, Crowther R, Weber D, Palermo R, Birktoft J, Biochemistry. 1998 Jun 2;37(22):7907-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9609683 9609683]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
Line 27: Line 36:
[[Category: zinc]]
[[Category: zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:14 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:19 2008''

Revision as of 09:12, 20 March 2008

Image:1fpp.gif


PDB ID 1fpp

Drag the structure with the mouse to rotate
, resolution 2.75Å
Sites:
Ligands: , and
Gene: FNTA, FNTB (Rattus norvegicus)
Coordinates: save as pdb, mmCIF, xml



PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE


Overview

The rat protein farnesyltransferase crystal structure has been solved by multiple isomorphous replacement methods at a resolution of 2.75 A. The three-dimensional structure, together with recent data on the effects of several mutations, led us to propose a model for substrate binding which differs from the model presented by Park et al. based on their independent structure determination [Park, H. -W., Boduluri, S. R., Moomaw, J. F., Casey, P. J., and Beese, L. S. (1997) Science 275, 1800-1804]. Both farnesyl diphosphate and peptide substrates can be accommodated in the hydrophobic active-site barrel, with the sole charged residue inside the barrel, Arg202 of the beta-subunit, forming a salt bridge with the negatively charged carboxy terminus of peptide substrates. Our proposals are based in part on the observation of electron density in the active site which can be modeled as bound farnesyl diphosphate carried through the enzyme purification. In addition, our model explains in structural terms the results of mutational studies which have identified several residues critical for substrate specificity and catalysis.

About this Structure

1FPP is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Protein farnesyltransferase: structure and implications for substrate binding., Dunten P, Kammlott U, Crowther R, Weber D, Palermo R, Birktoft J, Biochemistry. 1998 Jun 2;37(22):7907-12. PMID:9609683

Page seeded by OCA on Thu Mar 20 11:12:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fpp"
Personal tools