2qo3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qo3.jpg|left|200px]]<br /><applet load="2qo3" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2qo3.jpg|left|200px]]
-
caption="2qo3, resolution 2.59&Aring;" />
+
 
-
'''Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase'''<br />
+
{{Structure
 +
|PDB= 2qo3 |SIZE=350|CAPTION= <scene name='initialview01'>2qo3</scene>, resolution 2.59&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=CER:(2S, 3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE'>CER</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Erythronolide_synthase Erythronolide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94]
 +
|GENE= eryAII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 Saccharopolyspora erythraea])
 +
}}
 +
 
 +
'''Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2QO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CER:'>CER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Erythronolide_synthase Erythronolide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO3 OCA].
+
2QO3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_erythraea Saccharopolyspora erythraea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO3 OCA].
==Reference==
==Reference==
-
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase., Tang Y, Chen AY, Kim CY, Cane DE, Khosla C, Chem Biol. 2007 Aug;14(8):931-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17719492 17719492]
+
Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase., Tang Y, Chen AY, Kim CY, Cane DE, Khosla C, Chem Biol. 2007 Aug;14(8):931-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17719492 17719492]
[[Category: Erythronolide synthase]]
[[Category: Erythronolide synthase]]
[[Category: Saccharopolyspora erythraea]]
[[Category: Saccharopolyspora erythraea]]
Line 26: Line 35:
[[Category: phosphopantetheine]]
[[Category: phosphopantetheine]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:52 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:27:45 2008''

Revision as of 16:27, 20 March 2008


PDB ID 2qo3

Drag the structure with the mouse to rotate
, resolution 2.59Å
Ligands: , and
Gene: eryAII (Saccharopolyspora erythraea)
Activity: Erythronolide synthase, with EC number 2.3.1.94
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of [KS3][AT3] didomain from module 3 of 6-deoxyerthronolide B synthase


Overview

We report the 2.6 A X-ray crystal structure of a 190 kDa homodimeric fragment from module 3 of the 6-deoxyerthronolide B synthase covalently bound to the inhibitor cerulenin. The structure shows two well-organized interdomain linker regions in addition to the full-length ketosynthase (KS) and acyltransferase (AT) domains. Analysis of the substrate-binding site of the KS domain suggests that a loop region at the homodimer interface influences KS substrate specificity. We also describe a model for the interaction of the catalytic domains with the acyl carrier protein (ACP) domain. The ACP is proposed to dock within a deep cleft between the KS and AT domains, with interactions that span both the KS homodimer and AT domain. In conjunction with other recent data, our results provide atomic resolution pictures of several catalytically relevant protein interactions in this remarkable family of modular megasynthases.

About this Structure

2QO3 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase., Tang Y, Chen AY, Kim CY, Cane DE, Khosla C, Chem Biol. 2007 Aug;14(8):931-43. PMID:17719492

Page seeded by OCA on Thu Mar 20 18:27:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools