2qo3: Difference between revisions

Line 4:

==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.

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==

Line 14:

[[Category: Saccharopolyspora erythraea]]

[[Category: Single protein]]

[[Category: Cane, E.D.]]

[[Category: Cane, E D.]]

[[Category: Chen, Y.A.]]

[[Category: Chen, Y A.]]

[[Category: Khosla, C.]]

[[Category: Kim, C.Y.]]

[[Category: Kim, C Y.]]

[[Category: Tang, Y.]]

[[Category: ACT]]

Line 26:

[[Category: phosphopantetheine]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 13~~:47:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:52 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Saccharopolyspora erythraea]]
 [[Category: Single protein]]
-[[Category: Cane, E.D.]]
+[[Category: Cane, E D.]]
-[[Category: Chen, Y.A.]]
+[[Category: Chen, Y A.]]
 [[Category: Khosla, C.]]
-[[Category: Kim, C.Y.]]
+[[Category: Kim, C Y.]]
 [[Category: Tang, Y.]]
 [[Category: ACT]]
@@ Line 26: / Line 26: @@
 [[Category: phosphopantetheine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:47:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:52 2008''